Is the female speaker presence 4 in 29?
There are 11 messages totaling 3841 lines in this issue. > > Topics of the day: > > 1. xdscc12 Expires (2) > 2. 2 year BBSRC funded PDRA position at the University of Liverpool, UK > 3. Vacancy: structural biologist with cryo-EM expertise at GSK closing > date > 24th March (2) > 4. refinement / modeling of partly mobile domain > 5. PDRA position available in Leeds > 6. Cold Spring Harbor Asia conference on Membrane Proteins: Structure & > Function > 7. Fwd: how to calculate a difference map between two heterodimers in > heterotetrameric protein (3) > > ---------------------------------------------------------------------- > > Date: Fri, 10 Mar 2017 08:27:54 +0000 > From: Kay Diederichs <kay.diederi...@uni-konstanz.de> > Subject: Re: xdscc12 Expires > > Hi Carlos, > > sorry - the problem should be fixed now.; pls download a fresh copy. > Since I didn't find bugs for quite some time, the new binaries have no > expiration date. > > best wishes, > > Kay > > On Thu, 9 Mar 2017 21:18:12 +0100, Carlos CONTRERAS-MARTEL < > carlos.contreras-mar...@ibs.fr> wrote: > > >Hi CCP4BB > > > >My XDSGUI is reporting : > > > > > >xdscc12 -cdef -nbin 3 -t 1 XDS_ASCII.HKL > XDSCC12.LP > >expired > > > > > >So, downloaded again from the XDSWiKi link, but : > > > > > >xdscc12/20170309> ./xdscc12.rhel6.64 -h > >xdscc12 KD 2017-01-12. Academic use only; no redistribution. Expires > >2016-12-31. -h option shows options. > >Please cite Assmann, G., Brehm, W., Diederichs, K. (2016) J.Appl.Cryst. > >49, 1021-1028 > >usage: xdscc12 -dmin <lowres> -dmax <highres> -nbin <nbin> -mode <1 or > >2> -<abcdeftwz> FILE_NAME > >dmax (default 999A), dmin (default 1A) and nbin (default 10) have the > >usual meanings. > >mode can be 1 (equal volumes of resolution shells) or 2 (increasing > >volumes; default). > > -t: total oscillation (degree) to batch fine-sliced frames into > >other options can be combined (e.g. -def), and switch the following off: > > -a: individual isomorphous summary values > > -b: individual (Fisher-transformed) delta-CC1/2 values > > -c: individual delta-CC1/2 reflection numbers > > -d: individual anomalous summary values > > -e: individual (Fisher-transformed) delta-CC1/2ano values > > -f: individual delta-CC1/2ano reflection numbers > > -w: weighting of intensities with their sigmas > > -z: Fisher transformation of delta-CC1/2 values > > > > > >it seems to me also be a expired version ... > > > >Somebody know where I can find a newer-working version? > > > > > >All the best > > > > > >Carlos > > > >-- > > Carlos CONTRERAS MARTEL, Ph.D. > > (CR1 CNRS) > > > > carlos.contreras-mar...@ibs.fr > > > > "Bacterial Pathogenesis Group" > > Institut de Biologie Structurale > > UMR5075 CEA-CNRS-UGA > > > > IBS > > Campus EPN > > 71, avenue des Martyrs > > CS 10090 > > 38044 Grenoble CEDEX 9 > > FRANCE > > > > > > tel : (+33) (0)4 57 42 86 41 > > > >http://www.ibs.fr/groupes/groupe-pathogenie-bacterienne/?lang=fr > >http://www.ibs.fr/groups/bacterial-pathogenesis-group/?lang=en > > ------------------------------ > > Date: Fri, 10 Mar 2017 09:31:03 +0000 > From: "Antonyuk, Svetlana" <s.anton...@liverpool.ac.uk> > Subject: 2 year BBSRC funded PDRA position at the University of Liverpool, > UK > > THE UNIVERSITY OF LIVERPOOL > FACULTY OF HEALTH AND LIFE SCIENCES > INSTITUTE OF INTEGRATIVE BIOLOGY > DEPARTMENT OF BIOCHEMISTRY > POSTDOCTORAL RESEARCH ASSOCIATE GRADE 7 > £32,958 - £34,956 pa > An exciting opportunity has emerged in the Molecular Biophysics< > http://www.biophysics.liv.ac.uk/> group to work on a BBSRC-supported > project on structure-function-mechanism studies of Cu-nitrite reductase and > membrane bound nitric oxide (NO) reductase and the role of metabolon > complex formation in controlling levels of cytotoxic NO. The project will > link crystallographic studies with techniques to probe factors that control > delivery of electrons and protons to the active site of these enzymes. You > will be responsible for using established molecular biology procedures > underpinning the overexpression and purification of a number of enzymes and > their mutants including membrane proteins and undertake crystallographic, > spectroscopic and mechanistic aspects of the programme. You will have the > opportunity to spend up to 4 weeks in the RIKEN laboratories in Japan as > part of a collaborative programme alongside two PhD students working on > membrane-bound nitric oxide reductases. You should have a PhD in the area > of physics, chemistry, biological sciences or biophysics, with experience > in protein crystallography and practical knowledge of molecular biology > preferably with experience in membrane proteins. Excellent verbal and > written communication skills are essential. The post is available for 2 > years and the ability to commence immediately would be advantageous. > > Job Ref: 006744 > Closing Date: 11 April 2017 > > For full details and to apply online, please visit: > https://recruit.liverpool.ac.uk > > ------------------------------ > > Date: Fri, 10 Mar 2017 10:34:01 +0100 > From: Carlos CONTRERAS-MARTEL <carlos.contreras-mar...@ibs.fr> > Subject: Re: xdscc12 Expires > > Hi Kay > > > Thank you very much ... xdscc12 is working now perfectly ... so xdsgui > > > Best > > Carlos > > > On 03/10/17 09:27, Kay Diederichs wrote: > > Hi Carlos, > > > > sorry - the problem should be fixed now.; pls download a fresh copy. > > Since I didn't find bugs for quite some time, the new binaries have no > expiration date. > > > > best wishes, > > > > Kay > > > > On Thu, 9 Mar 2017 21:18:12 +0100, Carlos CONTRERAS-MARTEL < > carlos.contreras-mar...@ibs.fr> wrote: > > > >> Hi CCP4BB > >> > >> My XDSGUI is reporting : > >> > >> > >> xdscc12 -cdef -nbin 3 -t 1 XDS_ASCII.HKL > XDSCC12.LP > >> expired > >> > >> > >> So, downloaded again from the XDSWiKi link, but : > >> > >> > >> xdscc12/20170309> ./xdscc12.rhel6.64 -h > >> xdscc12 KD 2017-01-12. Academic use only; no redistribution. Expires > >> 2016-12-31. -h option shows options. > >> Please cite Assmann, G., Brehm, W., Diederichs, K. (2016) J.Appl.Cryst. > >> 49, 1021-1028 > >> usage: xdscc12 -dmin <lowres> -dmax <highres> -nbin <nbin> -mode <1 or > >> 2> -<abcdeftwz> FILE_NAME > >> dmax (default 999A), dmin (default 1A) and nbin (default 10) have the > >> usual meanings. > >> mode can be 1 (equal volumes of resolution shells) or 2 (increasing > >> volumes; default). > >> -t: total oscillation (degree) to batch fine-sliced frames into > >> other options can be combined (e.g. -def), and switch the following off: > >> -a: individual isomorphous summary values > >> -b: individual (Fisher-transformed) delta-CC1/2 values > >> -c: individual delta-CC1/2 reflection numbers > >> -d: individual anomalous summary values > >> -e: individual (Fisher-transformed) delta-CC1/2ano values > >> -f: individual delta-CC1/2ano reflection numbers > >> -w: weighting of intensities with their sigmas > >> -z: Fisher transformation of delta-CC1/2 values > >> > >> > >> it seems to me also be a expired version ... > >> > >> Somebody know where I can find a newer-working version? > >> > >> > >> All the best > >> > >> > >> Carlos > >> > >> -- > >> Carlos CONTRERAS MARTEL, Ph.D. > >> (CR1 CNRS) > >> > >> carlos.contreras-mar...@ibs.fr > >> > >> "Bacterial Pathogenesis Group" > >> Institut de Biologie Structurale > >> UMR5075 CEA-CNRS-UGA > >> > >> IBS > >> Campus EPN > >> 71, avenue des Martyrs > >> CS 10090 > >> 38044 Grenoble CEDEX 9 > >> FRANCE > >> > >> > >> tel : (+33) (0)4 57 42 86 41 > >> > >> http://www.ibs.fr/groupes/groupe-pathogenie-bacterienne/?lang=fr > >> http://www.ibs.fr/groups/bacterial-pathogenesis-group/?lang=en > > > -- > Carlos CONTRERAS MARTEL, Ph.D. > (CR1 CNRS) > > carlos.contreras-mar...@ibs.fr > > "Bacterial Pathogenesis Group" > Institut de Biologie Structurale > UMR5075 CEA-CNRS-UGA > > IBS > Campus EPN > 71, avenue des Martyrs > CS 10090 > 38044 Grenoble CEDEX 9 > FRANCE > > > tel : (+33) (0)4 57 42 86 41 > > http://www.ibs.fr/groupes/groupe-pathogenie-bacterienne/?lang=fr > http://www.ibs.fr/groups/bacterial-pathogenesis-group/?lang=en > > ------------------------------ > > Date: Fri, 10 Mar 2017 20:53:12 +0900 > From: Anindito Sen <andysen.to...@gmail.com> > Subject: Re: Vacancy: structural biologist with cryo-EM expertise at GSK > closing date 24th March > > Hello Dr. Chung, > > It was nice talking to you. I have submitted the application online. > However I have not received any email conformation. In any case, I am > attaching the screenshot of my submission below. > > Kindly acknowledge when you receive my application. > > Best Regards > > Andy > > > > > > > Anindito Sen. Ph.D > Scientist and Application Specialist in Biological Sciences > JEOL LTD. > 13F, Ohtemachi Nomura Bldg. > 2-1-1 Ohtemachi, Chiyoda-ku, Tokyo > 100-0004 > Tel: +81-3-62623563 > Fax: +81-3-6262-3577 > > www.jeol.com > > > On Mar 6, 2017, at 7:03 PM, Chun-wa Chung <chun-wa.h.ch...@gsk.com> > wrote: > > > > Job-posting - Seeking structural biologist with cryo-EM expertise at GSK > > > > A vacancy for a structural biologist with cryo-EM expertise has opened > up within the UK structural and biophysical sciences group at > GlaxoSmithKline R&D. Joining an experienced multi-disciplinary group, this > is an exciting opportunity for a motivated individual to complement and > help shape our current capabilities in the EM area. > > This is a permanent, full-time position suitable for a PhD degree holder > (or equivalent). > > > > To apply for this role and for further details, please click on the link > below (Vacancy no : WD106591) https://careers.peopleclick. > com/careerscp/client_gsk/external1931/gateway.do? > functionName=viewFromLink&jobPostId=330903&localeCode=en-us < > https://careers.peopleclick.com/careerscp/client_gsk/ > external1931/gateway.do?functionName=viewFromLink& > jobPostId=330903&localeCode=en-us> > > A full job description is also included at the end of this message. > > > > Applications for this vacancy are to be made online by 24th MARCH > > Informal inquiries can be sent to chun-wa.h.ch...@gsk.com <mailto: > chun-wa.h.ch...@gsk.com> > > Thank you for your interest, > > > > Chun-wa Chung > > > > UK Head Structural & Biophysics Sciences > > GlaxoSmithKline R&D > > Stevenage > > SG1 2NY > > Tel no: +44 1438 763342 > > email : chun-wa.h.ch...@gsk.com <mailto:chun-wa.h.ch...@gsk.com> > > > > > > > > Full Job Description (WD78277): > > GlaxoSmithKline is a world leading research-based pharmaceutical > company. We are focused around three core businesses: Pharmaceuticals, > Vaccines and GSK Consumer Healthcare. We have a significant global presence > with commercial operations in more than 150 countries, a network of 84 > manufacturing sites in 36 countries and large R&D centres in the UK, US, > Belgium and China. > > The UK Structural and Biophysical Sciences group is a multi-disciplinary > department within GSK R&D that provides molecular insights into drug > discovery for both small molecule and biopharmaceutical programs. > > > > We currently have an exciting opportunity for a laboratory-based > scientist with expertise in state-of-the-art electron microscopy techniques > to play an influential and key role in the application and development of > these methods across small molecule and therapeutic protein programs. This > individual will have extensive experience in the sample preparation and > optimisation processes necessary to produce high-quality molecular images > of protein structure, including direct experience of Cryo-EM methodologies. > Experience of data analysis and interpretation is also expected. Being > responsible for delivering structural insights to support program teams and > contributing to the wider protein structural and biophysical area by > identifying and driving forward improvements and innovations that advance > drug discovery projects, the individual must be a collaborative team player > able to work successfully with other scientists within the department and > within diverse teams. > > > > Key Responsibilities and Accountabilities: > > • Design and perform technical experiments in the EM area (sample > preparation, optimisation and analysis). > > • Document and communicate scientific results clearly and promptly. > > • Provide strong scientific lead to shape EM strategy within structural > biology and across therapeutic discovery programs. > > • Build EM capabilities and infrastructure through interactions with the > internal and external scientific community. > > • Maintain scientific excellence and lead in a rapidly evolving area > e.g. through interactions such as the FEI/LMB/Pharm consortium. > > • Become an integral team member of multiple project teams. > > > > Key Capabilities and Proficiency: > > 1. Technical expertise leading to Impact > > Evidence of specific and in depth knowledge of transmission electron > microscopy used as a structural technique, especially single particle > cryo-EM. A track record of its application to address scientific problems > relevant to pharmaceutical research. > > 2. Influence and Scientific awareness > > Evidence of engagement with external scientific environment including > the ability to identify and pursue opportunities that advance capabilities > within own research area. > > 3. Team work > > Demonstrable ability to both directly and indirectly influence and > impact the progression of programs of research and to work in > multi-disciplinary teams, displaying appropriate interpersonal skills and > team work > > > > > > > > > > > > This e-mail was sent by GlaxoSmithKline Services Unlimited > > (registered in England and Wales No. 1047315), which is a > > member of the GlaxoSmithKline group of companies. The > > registered address of GlaxoSmithKline Services Unlimited > > is 980 Great West Road, Brentford, Middlesex TW8 9GS. > > GSK monitors email communications sent to and from GSK in order to > protect GSK, our employees, customers, suppliers and business partners, > from cyber threats and loss of GSK Information. GSK monitoring is conducted > with appropriate confidentiality controls and in accordance with local laws > and after appropriate consultation. > > ------------------------------ > > Date: Fri, 10 Mar 2017 21:21:09 +0900 > From: Anindito Sen <andysen.to...@gmail.com> > Subject: Re: Vacancy: structural biologist with cryo-EM expertise at GSK > closing date 24th March > > Apologies to you All. > > The email got copied to every one. In any case its a junk for rest of you. > Kindly delete it, if you can. > > > Best Regards > > Andy > > > > Anindito Sen. Ph.D > > On Mar 10, 2017, at 9:17 PM, Vellieux Frédéric < > frederic.velli...@ibt.cas.cz> wrote: > > > > Hello, > > > > I am not “Dr Chung” and I haven’t received anything from you. Sorry to > disappoint you. > > > > Perhaps a “reply all” isn’t appropriate when replying to a ccp4bb > message ? I let you be the judge on that… > > > > Fred. > > > > From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK <mailto: > CCP4BB@JISCMAIL.AC.UK>] On Behalf Of Anindito Sen > > Sent: Friday, March 10, 2017 12:53 PM > > To: CCP4BB@JISCMAIL.AC.UK <mailto:CCP4BB@JISCMAIL.AC.UK> > > Subject: Re: [ccp4bb] Vacancy: structural biologist with cryo-EM > expertise at GSK closing date 24th March > > > > Hello Dr. Chung, > > > > It was nice talking to you. I have submitted the application online. > However I have not received any email conformation. In any case, I am > attaching the screenshot of my submission below. > > > > Kindly acknowledge when you receive my application. > > > > Best Regards > > > > Andy > > > > > > > > > > <image001.png> > > > > Anindito Sen. Ph.D > > Scientist and Application Specialist in Biological Sciences > > JEOL LTD. > > 13F, Ohtemachi Nomura Bldg. > > 2-1-1 Ohtemachi, Chiyoda-ku, Tokyo > > 100-0004 > > Tel: +81-3-62623563 > > Fax: +81-3-6262-3577 > > > > www.jeol.com <http://www.jeol.com/> > > > > On Mar 6, 2017, at 7:03 PM, Chun-wa Chung <chun-wa.h.ch...@gsk.com > <mailto:chun-wa.h.ch...@gsk.com>> wrote: > > > > Job-posting - Seeking structural biologist with cryo-EM expertise at GSK > > > > A vacancy for a structural biologist with cryo-EM expertise has opened > up within the UK structural and biophysical sciences group at > GlaxoSmithKline R&D. Joining an experienced multi-disciplinary group, this > is an exciting opportunity for a motivated individual to complement and > help shape our current capabilities in the EM area. > > This is a permanent, full-time position suitable for a PhD degree holder > (or equivalent). > > > > To apply for this role and for further details, please click on the link > below (Vacancy no : WD106591) https://careers.peopleclick. > com/careerscp/client_gsk/external1931/gateway.do? > functionName=viewFromLink&jobPostId=330903&localeCode=en-us < > https://careers.peopleclick.com/careerscp/client_gsk/ > external1931/gateway.do?functionName=viewFromLink& > jobPostId=330903&localeCode=en-us> > > A full job description is also included at the end of this message. > > > > Applications for this vacancy are to be made online by 24th MARCH > > Informal inquiries can be sent to chun-wa.h.ch...@gsk.com <mailto: > chun-wa.h.ch...@gsk.com> > > Thank you for your interest, > > > > Chun-wa Chung > > > > UK Head Structural & Biophysics Sciences > > GlaxoSmithKline R&D > > Stevenage > > SG1 2NY > > Tel no: +44 1438 763342 > > email : chun-wa.h.ch...@gsk.com <mailto:chun-wa.h.ch...@gsk.com> > > > > > > > > Full Job Description (WD78277): > > GlaxoSmithKline is a world leading research-based pharmaceutical > company. We are focused around three core businesses: Pharmaceuticals, > Vaccines and GSK Consumer Healthcare. We have a significant global presence > with commercial operations in more than 150 countries, a network of 84 > manufacturing sites in 36 countries and large R&D centres in the UK, US, > Belgium and China. > > The UK Structural and Biophysical Sciences group is a multi-disciplinary > department within GSK R&D that provides molecular insights into drug > discovery for both small molecule and biopharmaceutical programs. > > > > We currently have an exciting opportunity for a laboratory-based > scientist with expertise in state-of-the-art electron microscopy techniques > to play an influential and key role in the application and development of > these methods across small molecule and therapeutic protein programs. This > individual will have extensive experience in the sample preparation and > optimisation processes necessary to produce high-quality molecular images > of protein structure, including direct experience of Cryo-EM methodologies. > Experience of data analysis and interpretation is also expected. Being > responsible for delivering structural insights to support program teams and > contributing to the wider protein structural and biophysical area by > identifying and driving forward improvements and innovations that advance > drug discovery projects, the individual must be a collaborative team player > able to work successfully with other scientists within the department and > within diverse teams. > > > > Key Responsibilities and Accountabilities: > > • Design and perform technical experiments in the EM area (sample > preparation, optimisation and analysis). > > • Document and communicate scientific results clearly and promptly. > > • Provide strong scientific lead to shape EM strategy within structural > biology and across therapeutic discovery programs. > > • Build EM capabilities and infrastructure through interactions with the > internal and external scientific community. > > • Maintain scientific excellence and lead in a rapidly evolving area > e.g. through interactions such as the FEI/LMB/Pharm consortium. > > • Become an integral team member of multiple project teams. > > > > Key Capabilities and Proficiency: > > 1. Technical expertise leading to Impact > > Evidence of specific and in depth knowledge of transmission electron > microscopy used as a structural technique, especially single particle > cryo-EM. A track record of its application to address scientific problems > relevant to pharmaceutical research. > > 2. Influence and Scientific awareness > > Evidence of engagement with external scientific environment including > the ability to identify and pursue opportunities that advance capabilities > within own research area. > > 3. Team work > > Demonstrable ability to both directly and indirectly influence and > impact the progression of programs of research and to work in > multi-disciplinary teams, displaying appropriate interpersonal skills and > team work > > > > > > > > > > > > This e-mail was sent by GlaxoSmithKline Services Unlimited > > (registered in England and Wales No. 1047315), which is a > > member of the GlaxoSmithKline group of companies. The > > registered address of GlaxoSmithKline Services Unlimited > > is 980 Great West Road, Brentford, Middlesex TW8 9GS. > > > > GSK monitors email communications sent to and from GSK in order to > protect GSK, our employees, customers, suppliers and business partners, > from cyber threats and loss of GSK Information. GSK monitoring is conducted > with appropriate confidentiality controls and in accordance with local laws > and after appropriate consultation. > > > > ----- > > Upozornění: Není-li v této zprávě výslovně uvedeno jinak, má tato > E-mailová zpráva nebo její přílohy pouze informativní charakter. Tato > zpráva ani její přílohy v žádném ohledu Biotechnologický ústav AV ČR, v. v. > i. k ničemu nezavazují. Text této zprávy nebo jejích příloh není návrhem na > uzavření smlouvy, ani přijetím případného návrhu na uzavření smlouvy, ani > jiným právním jednáním směřujícím k uzavření jakékoliv smlouvy a nezakládá > předsmluvní odpovědnost Biotechnologického ústavu AV ČR, v. v. i. > > > > Disclaimer: If not expressly stated otherwise, this e-mail message > (including any attached files) is intended purely for informational > purposes and does not represent a binding agreement on the part of > Institute of Biotechnology CAS. The text of this message and its > attachments cannot be considered as a proposal to conclude a contract, nor > the acceptance of a proposal to conclude a contract, nor any other legal > act leading to concluding any contract; nor does it create any > pre-contractual liability on the part of Institute of Biotechnology CAS > > > > ------------------------------ > > Date: Fri, 10 Mar 2017 12:42:45 +0000 > From: "Kajander, Tommi A" <tommi.kajan...@helsinki.fi> > Subject: refinement / modeling of partly mobile domain > > Any hints on what might work for modeliing a domain that seems to be there > visible in part and parly not? > > (half ofan Ig-domain) - presumably the other end of the domain has larger > ensemble of coordinate > postions (attached from one end to other part of the same molecule and > neighbors in the crystal - and not at the other end, > causing maybe kind of swinging of it/positional disorder) - any good ideas > how to model this welcome... > > including the _whole domain model_ seems to drop R-factors but cant see > much additional density - maybe we just model the > missing part then for this structure if nothing else.. > > Thanks, > Tommi > > > > > ------------------------------ > > Date: Fri, 10 Mar 2017 13:45:53 +0000 > From: Glyn Hemsworth <g.r.hemswo...@leeds.ac.uk> > Subject: PDRA position available in Leeds > > Dear All, > > Can I please bring the PDRA opportunity that is available here in Leeds > once more to your attention as the deadline for applications - 21st March > 2017 is approaching. > > Funded by the BBSRC the position is available for an initial 2 year > period, with the possibility of extending to 4 years. The position will > suit someone interested in redox proteins, structural biology and > biotechnology. > > The full candidate brief can be downloaded from the following web address: > > https://jobs.leeds.ac.uk/FBSMB1100 > > To apply for the position please register for an account on the Leeds > website and submit a covering letter, together with a CV including details > of at least two references. > > Please feel free to get in touch with informal enquiries about the role. > Thanks and best wishes, > > Glyn > > ––––––––––––––––––––––––––––––––– > Glyn Hemsworth > Astbury Building, Room 10.107 > Faculty of Biological Sciences, > University of Leeds, Leeds, LS2 9JT, UK > Tel: (+44) 0113 3434 349 > Email: g.r.hemswo...@leeds.ac.uk<mailto:g.r.hemswo...@leeds.ac.uk> > > Research Fellow > > Are you an ambitious researcher looking for your next challenge? Do you > have an established background in Structural Biology, Biochemistry or > Chemistry? Do you want to further your career in one of the UKs leading > research intensive Universities? > > You will investigate the structure and function of a range of proteins, > and their complexes, as potential activators of a class of enzymes known as > lytic polysaccharide monooxygenases (LPMOs), (find out more in this recent > review<http://www.cell.com/trends/biotechnology/abstract/ > S0167-7799(15)00192-4?_returnURL=http%3A%2F%2Flinkinghub.elsevier.com% > 2Fretrieve%2Fpii%2FS0167779915001924%3Fshowall%3Dtrue>). LPMOs have > emerged as key enzymes in biomass conversion, both in nature and in the > applied setting of a biorefinery. Using a combination of structural, > biophysical, and biochemical methods we are seeking to characterise the > molecular mechanisms used in nature to shuttle electrons to LPMOs. The > knowledge gained from this research is of considerable interest from both a > fundamental and applied standpoint and will ultimately be used in protein > engineering approaches to produce more efficient enzyme systems to be used > in the biorefinery. > > Funded by the BBSRC, you will be based in the newly established laboratory > of Dr Glyn Hemsworth in the Faculty of Biological Sciences and the Astbury > Centre for Structural Molecular Biology. With the recent £17 million > investment in the Astbury Biostructure lab to complement the already superb > infrastructure for structural molecular biology, Leeds represents the > perfect environment for you to learn new techniques whilst contributing > vital knowledge towards realising the development of lignocellulosing > biofuels as a more sustainable energy source for the future. > > You should have, or be close to completing a PhD in Structural Biology, > Biochemistry, Chemistry or a related discipline, where practical experience > of cryo-electron microscopy or X-ray crystallography is essential. You will > be expected to show enthusiasm for engaging in inter-disciplinary research > and expanding your knowledge and expertise into new areas. Experience of > studying protein-protein interactions would also be an advantage. > > To explore the post further or for any queries you may have, please > contact: > > Glyn Hemsworth > > Tel: 0113 343 4349, email: g.r.hemswo...@leeds.ac.uk<mailto: > g.r.hemswo...@leeds.ac.uk> > > > Location: Leeds - Main Campus > Faculty/Service: Faculty of Biological Sciences > School/Institute: School of Molecular & Cellular Biology > Category: Research > Grade: Grade 7 > Salary: £32,004 to £38,183 p.a. > Contract Type: Fixed Term (Fixed term for 2 years due to funding - > optional 4 years) > Closing Date: Tuesday 21 March 2017 > Reference: FBSMB1100 > > ------------------------------ > > Date: Fri, 10 Mar 2017 14:00:45 +0000 > From: Martin Caffrey <martin.caff...@tcd.ie> > Subject: Cold Spring Harbor Asia conference on Membrane Proteins: > Structure & Function > > *Membrane Proteins: Structure & Function* > > Suzhou, China. May 15-19, 2017 > > Organized by: > > *Martin Caffrey,* Trinity College Dublin, Ireland > > *Nancy Carrasco,* Yale University, USA > > *Tian-Le Xu,* Shanghai Jiao Tong University, China > > *Ming Zhou,* Baylor College of Medicine, USA > > > > We are pleased to announce the *Cold Spring Harbor Asia conference on* > *Membrane > Proteins: Structure & Function* which will be held in Suzhou, China, > located approximately 60 miles west of Shanghai. The conference will begin > at *7:00 pm on the evening of Monday May 15, and will conclude after lunch > on May 19, 2017.* > > The conference will include up to eight oral sessions and four poster > sessions covering the latest findings across a range membrane protein > related topics. Many talks will be selected from submitted abstracts on the > basis of scientific merit and relevance. Social events throughout the > conference provide ample opportunity for informal interactions. > > *Major Topics* > > *1. Channels* > > > *2. Cryo-EM 3. Dynamics* > > *4. Emerging techniques* > > *5. Enzymes* > > *6. Functional characterization* > * 7. Transmembrane signalling* > > *8. Transporters* > > *Speakers* > > > *Martin Caffrey,* Trinity College Dublin, IRELAND > *Nancy Carrasco,* Yale Unviersity, USA > *Yifan Cheng,* University of California San Francisco, USA > *James Chou,* Harvard Medical School/National Center for Protein Science, > USA/CHINA > *Henry Colecraft,* Coumbia University, USA > *Raimund Dutzler,* University of Zurich, SWITZERLAND > *Karen Fleming,* Johns Hopkins University, USA > > *Xin Huang,* Amgen Inc., USA > > *Andy Kruse,* Harvard Medical School, USA > *Edmund Kunji,* Medical Research Council, UNITED KINGDOM > > *Zhenfeng Liu,* Institute of Biophysics, CAS, CHINA > > *Zhi-Jie Liu,* ShanghaiTech University, CHINA > *Kaspar Locher,* ETH Zurich, SWITZERLAND > > *Aashish Manglik,* Stanford University School of Medicine, USA > *Yasushi Okamura,* Osaka University, JAPAN > *Eduardo Perozo,* The University of Chicago, USA > *Scott Prosser,* University of Toronto Mississauga, CANADA > *Daniel Rosenbaum,* UT Southwestern Medical Center, USA > *Irina Serysheva,* UTHealth Medical School, USA > *Yigong Shi,* Tsinghua University, CHINA > *Roger Sunahara,* University of California, San Diego, USA > *Chris Tate,* MRC Laboratory of Molecular Biology, UNITED KINGDOM > *Kutti Vinothkumar,* MRC Laboratory of Molecular Biology, UNITED KINGDOM > *Tian-Le Xu,* Shanghai Jiao Tong University, CHINA > *Bailong Xiao,* Tsinghua University, CHINA > *Nieng Yan,* Tsinghua University, CHINA > > *Jian Yang,* Kunming Institute of Zoology, CHINA > > *Maojun Yang,* Tsinghua Univeristy, CHINA > *Ming Zhou,* Baylor College of Medicine, USA > > We encourage abstracts to contain new and unpublished materials. Abstracts > must be submitted electronically by the abstract deadline. Selection of > material for oral and poster presentation will be made by the organizers. > Status (talk/poster) of abstracts will be posted on this web site as soon > as decisions have been made by the organizers. > > *Fellowships * > We are eager to have as many young people as possible attend since they are > likely to benefit most from this meeting. A certain number of presentations > by graduate students and postdocs attending the conference will be selected > for fellowship (US $100-$500) awards. For more details, please visit > http://www.csh-asia.org/stipends.html > > > > We look forward to seeing you at Suzhou in May, 2017. > > Early Registration: 17 April 2017 > > Website: https://www.csh-asia.org/2017meetings/membrane.html > > > > -- > Martin Caffrey martin.caff...@tcd.ie > Schools of Medicine and Biochemistry & Immunology > Trinity Biomedical Sciences Institute, Trinity College Dublin > Room 5.62,152-160 Pearse St., Dublin 2, D02 R590, Ireland > http://www.tcd.ie/Biochemistry/research/m_caffrey.php > phone: +353-(0)1-896-4253; mobile: +353-(0)86-818-7704 > > ------------------------------ > > Date: Fri, 10 Mar 2017 14:24:30 -0800 > From: Oleg Zadvornyy <ol...@chemistry.montana.edu> > Subject: Fwd: how to calculate a difference map between two heterodimers > in heterotetrameric protein > > Dear All, > > > We are working on a tetrameric protein containing 2 heterodimers which are > related to each other by 2 fold symmetry. There are difference at the > active site between the two heterodimers in the crystals, and we would like > to make a difference map to compare one heterodimer to the other. I would > really appreciate your advise and suggestions how to perform this > comparison. > Thank you, > Oleg > > -- > Oleg A. Zadvornyy, PhD > > Institute of Biological Chemistry, > Washington State University > > 237 Clark Hall > Pullman, WA 99163 > > Tel: (509)-335-9837 > Lab: (509)-335-1958 > > ------------------------------ > > Date: Fri, 10 Mar 2017 22:48:34 +0000 > From: Eleanor Dodson <eleanor.dod...@york.ac.uk> > Subject: Re: Fwd: how to calculate a difference map between two > heterodimers in heterotetrameric protein > > This would be pretty difficult, but you know in COOT you can overlap the > maps for related chains / hetero dimers/ etc. ( Ask for NCS difference maps > in the DRAW menu ] The matrix which converts one set of coordinates to the > other is then applied to the electron density so you see the NCS relatd > maps together . I usually use the facility to get an averaged map of all > copies of a molecule to sped up rebuilding - fix a model with respect to > the average and do a fraction of the work - but you could also use it to > study the differences between the two active sites. > > In fact it may be possible to use this to get a true difference map, but it > is complicated and I cannot remember how to do it off the top of my head - > you have to output the NCS generated maps then mask the maps then use these > maps to generate structure factors, then set up a diff map calculation.. > Simpler to just inspect the differences by eye! > > Eleanor > > > On 10 March 2017 at 22:24, Oleg Zadvornyy <ol...@chemistry.montana.edu> > wrote: > > > Dear All, > > > > > > We are working on a tetrameric protein containing 2 heterodimers which > are > > related to each other by 2 fold symmetry. There are difference at the > > active site between the two heterodimers in the crystals, and we would > like > > to make a difference map to compare one heterodimer to the other. I would > > really appreciate your advise and suggestions how to perform this > > comparison. > > Thank you, > > Oleg > > > > -- > > Oleg A. Zadvornyy, PhD > > > > Institute of Biological Chemistry, > > Washington State University > > > > 237 Clark Hall > > Pullman, WA 99163 > > > > Tel: (509)-335-9837 <(509)%20335-9837> > > Lab: (509)-335-1958 <(509)%20335-1958> > > > > ------------------------------ > > Date: Fri, 10 Mar 2017 18:24:51 -0500 > From: Phil Jeffrey <pjeff...@princeton.edu> > Subject: Re: Fwd: how to calculate a difference map between two > heterodimers in heterotetrameric protein > > Tricky - perhaps this could be viewed as "anti-averaging" methodologically. > > Use USF programs MAMA, IMP to generate a mask and optimize the NCS > operator (or skip this step if you feel you know yours accurately) > > Use CCP4's MAPROT to rotate the map of one monomer onto the other > > Conceivably use USF program COMDEM to create the "difference map" > assuming it will tolerate a weighting of -1. Or perhaps MAPROT will > take a negative scale. Or MAPMASK, or.... there's a range of map > manipulation programs that can scale an input map, but I've never tried > to invert one. Unless you actually wanted Fourier coefficients it > shouldn't be impossible to create a masked volume of the difference > between two maps after rotating one of them. > > Phil Jeffrey > Princeton > > On 3/10/17 5:24 PM, Oleg Zadvornyy wrote: > > Dear All, > > > > > > We are working on a tetrameric protein containing 2 heterodimers which > > are related to each other by 2 fold symmetry. There are difference at > > the active site between the two heterodimers in the crystals, and we > > would like to make a difference map to compare one heterodimer to the > > other. I would really appreciate your advise and suggestions how to > > perform this comparison. > > Thank you, > > Oleg > > > > -- > > Oleg A. Zadvornyy, PhD > > > > Institute of Biological Chemistry, > > Washington State University > > > > 237 Clark Hall > > Pullman, WA 99163 > > > > Tel: (509)-335-9837 > > Lab: (509)-335-1958 > > ------------------------------ >
