[ccp4bb] PhD position available at Umeå University, Sweden

[Elisabeth Sauer-Eriksson]

A PhD position in structural biology/biochemistry is available in my group.
More information can be found at:

http://www.umu.se/english/about-umu/open-positions?languageId=1

search for "PhD-position in Chemistry (with focus on Biochemistry/Structural 
Biology)"
Regards
Elisabeth Sauer-Eriksson


Description
This PhD position is part of a larger research project where we aim to design 
molecules - so-called inhibitors - that block bacterial virulence, i.e. the 
bacteria's ability to infect host cells. By not killing the bacteria, but 
rather blocking their virulence, the risk of developing resistance to the 
inhibitors is significantly reduced. Primarily, your studies will focus on 
identifying inhibitors that target the regulatory protein, PrfA, from the 
pathogen Listeria monocytogenes, but your studies will also include proteins 
from other pathogenic bacteria. The project group includes structural 
biologists, organic chemists and molecular biologists at Umeå University. The 
project can be described as a drug discovery project where your role is to 
determine and analyze structures of protein-molecule complex so that they can 
form the foundation for design of new and improved molecules. The structural 
studies will mainly be performed using X-ray crystallographic methods. 
Synthesis of new molecules and the effect of these on bacteria in vivo are made 
by our collaboration partners.

You can read more about the project in:

Attenuating Listeria monocytogenes Virulence by Targeting the Regulatory 
Protein PrfA.   Good JA, 
Andersson C, Hansen S, Wall J, Krishnan KS, Begum A, Grundström C, Niemiec MS, 
Vaitkevicius K, Chorell E, Wittung-Stafshede P, Sauer UH, Sauer-Eriksson AE, 
Almqvist F, Johansson J.  Cell Chem Biol. 2016, 23(3):404-14.

[ccp4bb] Structural biologist position at Sanofi

[Ronnie]

Description
Sanofi Genzyme focuses on developing specialty treatments for debilitating 
diseases that are often difficult to diagnose and treat, providing hope to 
patients and their families.Genzyme Corporation (a Sanofi company) and its U.S. 
affiliates are Equal Opportunity and Affirmative Action employers committed to 
a culturally diverse workforce. All qualified applicants will receive 
consideration for employment without regard to race; color; creed; religion; 
national origin; age; ancestry; nationality; marital, domestic partnership or 
civil union status; sex, gender, gender identity or expression; affectional or 
sexual orientation; disability; veteran or military status or liability for 
military status; domestic violence victim status; atypical cellular or blood 
trait; genetic information (including the refusal to submit to genetic testing) 
or any other characteristic protected by law.A highly motivated candidate is 
sought to join the Protein Engineering group within the Biologic Research 
Department. The individual will carry out purification and crystallization of 
biologics targets, especially antibody-antigen complexes; determining the 
structures of protein-ligands; analyzing and interpreting the structures; 
presenting and communicating the results to other science teams. A successful 
candidate will perform complex analytical procedures, and also contribute to 
the overall project design and implementation of new technology. 

Qualifications
Basic Qualifications:Ph.D. in protein crystallography or equivalent with less 
than 5 years of postdoctoral experience. Proven in-depth knowledge and 
expertise in protein structural biology demonstrated preferably through 
principal authorship in peer-reviewed publication(s). Specifically, candidates 
must have extensive experience in protein construct optimization, protein 
purification, crystallization, data collection and structure determination with 
strong protein chemistry skills. Expertise in common crystallographic software 
such as CCP4, HKL, Phenix is required.Preferred Qualifications:Strong and 
consistent written and oral communication ability. Familiarity with lab 
robotics and automation and other protein biophysical characterization 
techniques is preferred. Knowledge of antibody structures and experience with 
electron microscopy is also desirable.
To apply, please go to: Scientist, Biologics and Protein Engineering Job at 
Framingham at Sanofi
Thanks,
  
|  
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Scientist, Biologics and Protein Engineering Job at Framingham at Sanofi
 Learn more about applying for Scientist, Biologics and Protein Engineering at 
Sanofi  |  |

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Re: [ccp4bb] Crystals grow at the bottom of the tube.

[Hargreaves, David]

I have been presented with crystals grown in nmr tubes on two separate 
occasions. Both diffracted very well and thankfully, neither required a 
magnetic field for optimisation. On the first occasion I did use the initial 
sample as a seed stock.

Best wishes,

David

From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of kiki
Sent: 18 October 2016 11:42
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Crystals grow at the bottom of the tube.

Dear all users,

 I got my crystals at the bottom of the tube on ice just before I started to 
screen crystals. Those crystals' shapes were good but easy to melt when I 
harvested them. I shot these crystals. They only diffracted to 7A to 8A. Has 
anyone ever met this situation before? How to improve?

Thanks,
Lingyuan


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Re: [ccp4bb] Crystals grow at the bottom of the tube.

[mesters]

Yes, it is many years ago, a large protein batch (50 ml or so) stored in 
the cold room that produced an impressive layer of crystals at the 
bottom of the flask.
One student at that time tested many crystals and found only a few that 
diffracted to atomic (!) resolution.


Crystallization is a usefull methodology for protein purification! What 
I would do is to harvest these crystals (often more pure protein than in 
the stock solution), dissolve them and try to grow new crystals as 
proposed by Artem.


Good luck!

Jeroen


Am 18.10.16 um 12:41 schrieb kiki:

Dear all users,

 I got my crystals at the bottom of the tube on ice just before I 
started to screen crystals. Those crystals' shapes were good but easy 
to melt when I harvested them. I shot these crystals. They only 
diffracted to 7A to 8A. Has anyone ever met this situation before? How 
to improve?


Thanks,
Lingyuan


--
Dr.math. et dis. nat. Jeroen R. Mesters
Deputy, Senior Researcher & Lecturer
Program Coordinator /Infection Biology/ 



Institute of Biochemistry, University of Lübeck
Ratzeburger Allee 160, 23538 Lübeck, Germany
phone: +49-451-31013105 (secretariate -31013101)
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http://www.iobcr.org 


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and which will not, speak then to me who neither beg nor fear 
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