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Sent via the Samsung GALAXY S®4, an AT&T 4G LTE smartphone <div>-------- Original message --------</div><div>From: CCP4BB automatic digest system <lists...@jiscmail.ac.uk> </div><div>Date:08/14/2014 6:00 PM (GMT-06:00) </div><div>To: CCP4BB@JISCMAIL.AC.UK </div><div>Subject: CCP4BB Digest - 13 Aug 2014 to 14 Aug 2014 (#2014-220) </div><div> </div>There are 17 messages totaling 1766 lines in this issue. Topics of the day: 1. Off topic: Cloning multi genes/multi cistronic in yeast 2. software/web server to determine ligand volume 3. Question about Pilatus2M with denzo and xdisp 4. Difference between different b factors values (2) 5. CC-half value 6. AW: [ccp4bb] Difference between different b factors values 7. Twinning in space group Pc 8. Kinase postdoc positions available at SGC, Oxford University 9. desiring untouched ligand (2) 10. CC-half value ?? (3) 11. monomer/dimer protein 12. dynapro DLS cuvettes (2) ---------------------------------------------------------------------- Date: Wed, 13 Aug 2014 15:51:57 -0700 From: Karsten Thierbach <thier...@caltech.edu> Subject: Re: Off topic: Cloning multi genes/multi cistronic in yeast Hey, in my old lab we developed a system to express two proteins from one plasmid using the before mentioned GAL1-10 Promoter. Giving the use of different plasmids with different selection markers, coexpression of multiple proteins is possible in yeast. The system was used in a study published in Structure last year and you could contact my old lab to request plasmids. We used a TRP1 and a LEU2 plasmid and coexpressed three proteins in this study, but it is easily extendable to at least 4 proteins. You can find the paper here: http://www.ncbi.nlm.nih.gov/pubmed/23954503 To receive plasmids from the study, please contact Ed Hurt, the corresponding author at the BZH in Heidelberg/Germany. I stumbled across a similar system recently, which is also based on the GAL promoter, but don't find the reference now... Good luck, Karsten Am 13.08.2014 15:31, schrieb Chris Putnam: > On 8/13/14 2:29 PM, Theresa Hsu wrote: >> Dear all >> >> One of my human membrane proteins have been described to interact >> with additional subunits for its activity. To obtain functional form >> in yeast (Saccharomyces), I can think of two approach of either >> cloning all the subunits under one promoter or reconstitute in vitro. >> >> For the first option, what is the length of base pairs between the >> stop codon of one gene and the start of Kozak sequence for the next >> one? Is there any preference for the order so that only one subunit >> is His tagged? >> >> Second option will need multiple purification steps and some trials >> with protein ratios. Is this better? >> >> > > Natively, Saccharomyces does not have operons. And I am unaware of > operon-like constructs (single promoter with multiple genes oriented > in the same direction) working in Saccharomyces. (The GAL1-10 > divergent promoter is probably the closest analog, but this involves > transcription of the GAL1 and GAL10 genes that are encoded on opposite > strands in opposite orientations.) > > For multiprotein complexes, one strategy for in vivo complex assembly > is to encode each protein (with its own promoter) on separate plasmid > (with distinct selectable markers) and transform them all into the > same strain. This avoids the problems of in vitro reconstitution of > the complex as well as the problem of subunits that cannot be stably > expressed alone. > > Chris. -- Karsten Thierbach, Dr. rer. nat. California Institute of Technology Division of Chemistry & Chemical Engineering Hoelz laboratory 1200 E. California Blvd., M/C 147-75 Pasadena, CA 91125, U.S.A. ------------------------------ Date: Wed, 13 Aug 2014 17:19:14 -0600 From: Javier Gonzalez <bio...@gmail.com> Subject: Re: software/web server to determine ligand volume You can calculate volumes and much more, here: http://www.molinspiration.com/cgi-bin/properties Javier On Wed, Aug 13, 2014 at 12:06 AM, sreetama das <somon_...@yahoo.co.in> wrote: > Dear all, > Is there any software or web server available to calculate the volume of a > ligand if the ligand coordinates are provided? > Google seems to come up only with options to calculate protein cavity > volume. > > Thanks in advance, > Sreetama Das, > phd student, > Physics, IISc > -- Javier M. Gonzalez, PhD. Protein Crystallography Station Bioscience Division Bioenergy and Biome Sciences Group (B-11) Los Alamos National Laboratory TA-3, Building 4200, Room 202B Mailstop T007 Los Alamos, NM 87545 Phone: +1 (505) 667-9376 LinkedIn <http://www.linkedin.com/pub/javier-gonz%C3%A1lez/22/7b/83a> Email <bio...@gmail.com> ------------------------------ Date: Thu, 14 Aug 2014 09:25:15 +0300 From: Meytal Landau <landau.mey...@gmail.com> Subject: Re: Question about Pilatus2M with denzo and xdisp For all who are interested in this issue: HKL people solved the problem. The command for xdisp and denzo is:ccd 2m-pilatuscbf The def.site is also attached. Thanks to all who gave good advices, (and thanks Marcin for solving the problem), Meytal --------------------------- Meytal Landau, Ph.D. Assistant Professor Faculty of Biology Technion, Israel Institute of Technology Haifa, Israel E-mail :mlan...@technion.ac.il www: http://mlandau.net.technion.ac.il/ Tel office/lab:+972-77-8871965/4 On Aug 12, 2014, at 12:22 PM, Meytal Landau <landau.mey...@gmail.com> wrote: > Hello all, > > I am trying to use DENZO (the command-line program) and XDISP for images > coming from Pilatus 2M (ESRF ID-23-2). > Does anyone know the detector’s definitions? > I tried “ccd unsupported-m225” but it doesnt fit. > > Thanks > > Meytal > > --------------------------- > Meytal Landau, Ph.D. > Assistant Professor > Faculty of Biology > Technion, Israel Institute of Technology > Haifa, Israel > E-mail :mlan...@technion.ac.il > www: http://mlandau.net.technion.ac.il/ > Tel office/lab:+972-77-8871965/4 > > > > ------------------------------ Date: Thu, 14 Aug 2014 14:00:37 +0530 From: Faisal Tarique <faisaltari...@gmail.com> Subject: Difference between different b factors values Dear all I request you to please tell me the difference between wilson B-factor and average B, all atoms ?? I have two structures one native at 2A resolution, having mean b factor of 24 and the other a complex structure of the same protein with a ligand (at 2.6A resolution) has mean b factor of 23..Why there is a difference in the b factor for these two coordinates with the later having (low resolution) lower value than the previous (high resolution)..?? is this a normal phenomenon or the stability is due to bound ligand molecule, which is stabilizing the whole structure ?? Please pour some light in this direction.. -- Regards Faisal School of Life Sciences JNU ------------------------------ Date: Thu, 14 Aug 2014 14:10:05 +0530 From: Faisal Tarique <faisaltari...@gmail.com> Subject: CC-half value Dear all How CC-half value of a data set determines the resolution limit for the data processing ?? Although much we know about the Rsym and I/Isig values of the highest resolution shell while processing the data, what are the parameters we need to check related to CC-half values ?? -- Regards Faisal School of Life Sciences JNU ------------------------------ Date: Thu, 14 Aug 2014 09:15:41 +0000 From: herman.schreu...@sanofi.com Subject: AW: [ccp4bb] Difference between different b factors values Dear Faisal, The Wilson B-factor is the B-factor of the diffraction data and is calculated by the data processing software. The B-factor of the atoms is produced by the refinement program. Ideally the Wilson B (B-factor of the data) and average B of all atoms (B-factor of the model) should be very similar. In a perfect world, your resolution limit is determined by the Wilson B-factor (amount of crystal disorder) and one expects a low Wilson B-factor for high resolution data and a high Wilson B-factor for low resolution data. I think there are even papers were people have calculated the relation between Wilson B-factor and resolution limit. In practice, for low-resolution data the calculated B-factor may not be very well defined since it also depends on the scale factor. Also for high-resolution models, many water molecules with high B-factors may be included, while for low-resolution models only a few waters with low B-factors may have been included skewing the calculated average B. The first thing to check would be the Wilson B-factors and that they do not deviate too much from the average B-factors. I would be cautious drawing too many conclusions from the average B-values, since they reflect the crystal quality. E.g. if the cryoprotectant for one of the crystals was not optimal, you may get a high average B-value which has nothing to do with the stability of your protein. Best, Herman Von: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] Im Auftrag von Faisal Tarique Gesendet: Donnerstag, 14. August 2014 10:31 An: CCP4BB@JISCMAIL.AC.UK Betreff: [ccp4bb] Difference between different b factors values Dear all I request you to please tell me the difference between wilson B-factor and average B, all atoms ?? I have two structures one native at 2A resolution, having mean b factor of 24 and the other a complex structure of the same protein with a ligand (at 2.6A resolution) has mean b factor of 23..Why there is a difference in the b factor for these two coordinates with the later having (low resolution) lower value than the previous (high resolution)..?? is this a normal phenomenon or the stability is due to bound ligand molecule, which is stabilizing the whole structure ?? Please pour some light in this direction.. -- Regards Faisal School of Life Sciences JNU ------------------------------ Date: Thu, 14 Aug 2014 11:39:34 +0200 From: Tim Gruene <t...@shelx.uni-ac.gwdg.de> Subject: Re: Difference between different b factors values Dear Faisal, at 2.6A resolution I would not call 23A^2 and 24A^2 'a difference', rather a fluctuation. Parameters are not totally independent from each other and not from experimental issues. It most likely also make a difference which program you use. Some program has a upper cut-off of 100-200 (which I think is reasonable) while I have seen atoms in the PDB with B-values in the region of 500A^2 (which is close to saying the resolution of the data set is less than 5A...). Best, Tim On 08/14/2014 10:30 AM, Faisal Tarique wrote: > Dear all > > I request you to please tell me the difference between wilson B-factor and > average B, all atoms ?? I have two structures one native at 2A resolution, > having mean b factor of 24 and the other a complex structure of the same > protein with a ligand (at 2.6A resolution) has mean b factor of 23..Why > there is a difference in the b factor for these two coordinates with the > later having (low resolution) lower value than the previous (high > resolution)..?? is this a normal phenomenon or the stability is due to > bound ligand molecule, which is stabilizing the whole structure ?? Please > pour some light in this direction.. > -- Dr Tim Gruene Institut fuer anorganische Chemie Tammannstr. 4 D-37077 Goettingen GPG Key ID = A46BEE1A ------------------------------ Date: Thu, 14 Aug 2014 12:21:22 +0200 From: Navdeep Sidhu <nsi...@shelx.uni-ac.gwdg.de> Subject: Re: Twinning in space group Pc Dear Kristof, Apart from things pointed out, a possibility to consider would also be the presence of two different crystal types--of different compounds--in the same reaction vessel. Best regards, Navdeep --- On Wed, Aug 13, 2014 at 11:00:18AM +0200, Kristof Van Hecke wrote: > Dear, > > I’m struggling with the following (small molecule) problem: > > We are trying to solve the structure of a metal-organic framework containing > a chiral compound. > The space group is most probably Pc, but when refining, SHELX gives the error > “Possible racemic twin or wrong absolute structure - try TWIN refinement”. > As we know our compound is enantiopure, a racemic twin is very unlikely. In > this regard, also a centro-symmetric space group is not possible (although > CrysAlisPro always gives P2/c as the proper space group). As a matter of > fact, trying different space groups is not solving the problem. > > The second problem is that half of the structure is visible, but the other > half is completely not clear. Refinement is not possible at all (R-value of > 33%). > When running TwinRotMat (Platon), I get the following possible 2-fold twin > axes: > > 2-axis ( 0 1 -1 ) [ -2 5 -4 ], Angle () [] = 2.31 Deg, Freq = 14 > ************* > (-0.992 -0.019 0.015) (h1) (h2) Nr Overlap = 84 > (-0.430 0.075 -0.860) * (k1) = (k2) BASF = 0.96 > ( 0.459 -1.146 -0.083) (l1) (l2) DEL-R =-0.064 > > 2-axis ( 0 1 1 ) [ 2 5 4 ], Angle () [] = 2.31 Deg, Freq = 15 > ************* > (-0.992 0.019 0.015) (h1) (h2) Nr Overlap = 229 > ( 0.430 0.075 0.860) * (k1) = (k2) BASF = 0.94 > ( 0.459 1.146 -0.083) (l1) (l2) DEL-R =-0.050 > > 2-axis ( 1 0 -2 ) [ 3 0 -2 ], Angle () [] = 0.54 Deg, Freq = 19 > ************* > (-0.136 0.000 -0.576) (h1) (h2) Nr Overlap = 992 > ( 0.000 -1.000 0.000) * (k1) = (k2) BASF = 0.86 > (-1.703 0.000 0.136) (l1) (l2) DEL-R =-0.030 > > 2-axis ( 1 2 -1 ) [ 5 5 -1 ], Angle () [] = 0.39 Deg, Freq = 13 > ************* > (-0.380 0.620 -0.124) (h1) (h2) Nr Overlap = 854 > ( 1.256 0.256 -0.251) * (k1) = (k2) BASF = 0.88 > (-0.617 -0.617 -0.877) (l1) (l2) DEL-R =-0.019 > > However, none of these do actually improve the refinement. > > > Has anyone encountered possible twinning/twin laws in Pc please? > Or any other suggestions are most welcome? > > > Thank you very much > > Kristof --- Navdeep Sidhu Dept. of Neuropediatrics University of Goettingen Germany Email: nsi...@shelx.uni-ac.gwdg.de Homepage: http://shelx.uni-ac.gwdg.de/~nsidhu --- ------------------------------ Date: Thu, 14 Aug 2014 11:04:11 +0000 From: Alex Bullock <alex.bull...@sgc.ox.ac.uk> Subject: Kinase postdoc positions available at SGC, Oxford University Two postdoc positions are available at the SGC labs at the University of Oxford to work on the structure and inhibition of human protein kinases. The first is a Wellcome Trust funded project (CAMSEED) working with Stefan Knapp to develop inhibitors against the protein kinase CaMK1D in breast cancer. The second position with Alex Bullock is to characterise the structure and inhibition of kinases implicated in Huntington's disease. Applicants interested in either position can apply using the posting on jobs.ac.uk linked below (closing date 12 noon on 26 August 2014): http://www.jobs.ac.uk/job/AJK107/postdoctoral-scientist-structural-biology/ ------------------------------ Date: Thu, 14 Aug 2014 11:11:20 -0400 From: Remie Fawaz-Touma <remiefa...@gmail.com> Subject: Re: desiring untouched ligand Thank you Dr. Murshudov for the information. But please I still need help. In restrained refinement, I could not find where to enter the residues I want to restrict from moving much. I was only able to find that in rigid body refinement, so I tried it and got a higher R factor than the initial file (before refinement). Is it normal to get a higher R factor when doing rigid body refinement? if not, any suggestion regarding what could be wrong? Is there a way to restrict one chain or part of a chain from moving much while doing restrained refinement? Thank you for any input, Remie On Aug 13, 2014, at 10:48 AM, Garib Murshudov <ga...@mrc-lmb.cam.ac.uk> wrote: > Hi Remie, > > You can add harmonic restraints for parts you do not want to move too much. > Instructions could be found here: > http://www2.mrc-lmb.cam.ac.uk/groups/murshudov/content/refmac/refmac_keywords.html#Harmonic > > > Regards > Garib > > > On 13 Aug 2014, at 15:44, Remie Fawaz-Touma <remiefa...@gmail.com> wrote: > >> Hi everyone, >> >> Does anyone know of a way to refine with CCP4 - Refmac5 (restrained >> refinement is what I do) fixing a part of the the ligand? >> >> Thank you very much for your input, >> >> Remie > > Dr Garib N Murshudov > MRC-LMB > Francis Crick Avenue > Cambridge > CB2 0QH UK > Web http://www.mrc-lmb.cam.ac.uk, > http://www2.mrc-lmb.cam.ac.uk/groups/murshudov/ > > > ------------------------------ Date: Thu, 14 Aug 2014 11:39:19 -0400 From: Philip Kiser <p...@case.edu> Subject: Re: desiring untouched ligand Remie, Look at the following webpage: http://www.ysbl.york.ac.uk/refmac/data/refmac_news.html The harmonic restraints need to go into a "keyword" file that is uploaded to the "refmac keyword field" field in the GUI. Philip On Thu, Aug 14, 2014 at 11:11 AM, Remie Fawaz-Touma <remiefa...@gmail.com> wrote: > Thank you Dr. Murshudov for the information. But please I still need help. > > In restrained refinement, I could not find where to enter the residues I > want to restrict from moving much. I was only able to find that in rigid > body refinement, so I tried it and got a higher R factor than the initial > file (before refinement). > > Is it normal to get a higher R factor when doing rigid body refinement? if > not, any suggestion regarding what could be wrong? > > *Is there a way to restrict one chain or part of a chain from moving much > while doing restrained refinement? * > > Thank you for any input, > > Remie > > On Aug 13, 2014, at 10:48 AM, Garib Murshudov <ga...@mrc-lmb.cam.ac.uk> > wrote: > > Hi Remie, > > You can add harmonic restraints for parts you do not want to move too > much. Instructions could be found here: > > http://www2.mrc-lmb.cam.ac.uk/groups/murshudov/content/refmac/refmac_keywords.html#Harmonic > > > Regards > Garib > > > On 13 Aug 2014, at 15:44, Remie Fawaz-Touma <remiefa...@gmail.com> wrote: > > Hi everyone, > > Does anyone know of a way to refine with CCP4 - Refmac5 (restrained > refinement is what I do) fixing a part of the the ligand? > > Thank you very much for your input, > > Remie > > > Dr Garib N Murshudov > MRC-LMB > Francis Crick Avenue > Cambridge > CB2 0QH UK > Web http://www.mrc-lmb.cam.ac.uk, > http://www2.mrc-lmb.cam.ac.uk/groups/murshudov/ > > > > > ------------------------------ Date: Fri, 15 Aug 2014 01:39:48 +0530 From: Faisal Tarique <faisaltari...@gmail.com> Subject: CC-half value ?? Dear all How CC-half value of a data set determines the maximum resolution limit during data processing ?? Although much we know about the Rsym and I/Isig values of the highest resolution shell while processing the data, what are the parameters we need to check related to CC-half values ?? -- Regards Faisal School of Life Sciences JNU ------------------------------ Date: Thu, 14 Aug 2014 21:04:04 +0000 From: conan仙人指路 <conan_...@hotmail.com> Subject: Re: CC-half value ?? Hi Faisal, CC-half standard is valuable in evaluating the cut-off of highest resolution. Sometimes even if I/sigI is close to 1 and completeness is not as high, if CC-half is still significant, it may be worth incorporate the extra high-res shell data and extend the resolution. Again, if only the reliability and unbias are carefully confirmed, and the apparent significant CC-half is not due to an artifact of some other factors like ice ring etc.(Ref: Karplus PA and Diederichs K. 2012 Science 336, 1030-1033 https://www.pubmed.com/pubmed/22628654) It has yet to be appreciated by most population of the crystallography society, unlike the I/sigI, completeness, Rsym. In particular, Rsym has gradually less a direct measurement of the data quality and or determinant of resolution cut-off. Best,Conan Hongnan Cao, Ph.D.Department of BiochemistryRice University Date: Fri, 15 Aug 2014 01:39:48 +0530 From: faisaltari...@gmail.com Subject: [ccp4bb] CC-half value ?? To: CCP4BB@JISCMAIL.AC.UK Dear all How CC-half value of a data set determines the maximum resolution limit during data processing ?? Although much we know about the Rsym and I/Isig values of the highest resolution shell while processing the data, what are the parameters we need to check related to CC-half values ?? -- Regards Faisal School of Life Sciences JNU ------------------------------ Date: Thu, 14 Aug 2014 17:14:11 -0400 From: Shane Caldwell <shane.caldwel...@gmail.com> Subject: Re: monomer/dimer protein Hi Todd, Do you mean reversible or irreversible dimers? If the binding is reversible, then once crystal growth starts, Le Chatelier's principle should take over, pull the equilibrium toward monomer, and you should see minimal impact of dimer on your "monomer crystals". The same would be true in reverse for proteins that pack as dimers or higher-order oligos in the crystal. If the dimer formation is irreversible (ie. disulfide-mediated, domain-swapped, ....), they can be considered a chemically distinct entity and could indeed disrupt crystal packing. The most thorough treatment of the subject I know of is Chapter 8 of McPherson, although I don't think it addresses dimers specifically, just nonspecific aggregates. Perhaps still a place to start? Shane Caldwell McGill University On Wed, Aug 13, 2014 at 5:40 PM, Todd Jason Green <tgr...@uab.edu> wrote: > Hello All- > > I am interested in monomer/dimer contamination when building a crystal > lattice, ie. if you are building a crystal lattice with a monomeric species > of protein, incorporation of dimers may yield lattice or surface defects. > This species may be considered a macromolecular contaminant. I have read a > few papers on this subject, a couple are listed here: > > I. Yoshizaki et al. / Journal of Crystal Growth 290 (2006) 185–191 > > Caylor CL1, Dobrianov I, Lemay SG, Kimmer C, Kriminski S, Finkelstein KD, > Zipfel W, Webb WW, Thomas BR, Chernov AA, Thorne RE. Proteins. 1999 Aug > 15;36(3):270-81. > > In each of the studies that I have read, lysozyme is the model protein for > these studies. I have not seen studies thus far that have been done with > other proteins. Can anyone point me toward other studies, specifically > non-lysozyme studies, where incorporation of two different oligomerization > states has been shown to yield crystals with higher level of defects? > Microscopy studies of such would be great too. > > Thanks in advance- > Todd > ------------------------------ Date: Thu, 14 Aug 2014 16:35:01 -0500 From: Gloria Borgstahl <gborgst...@gmail.com> Subject: dynapro DLS cuvettes Does any one know of a source of these cuvettes? Protein Solution doesn't exist anymore and Wyatt no longer has these. ------------------------------ Date: Thu, 14 Aug 2014 17:44:53 -0400 From: Roger Rowlett <rrowl...@colgate.edu> Subject: Re: CC-half value ?? Exactly. Aimless will give you suggested resolution cutoffs based on CC 1/2 in the log file. Roger Rowlett On Aug 14, 2014 5:04 PM, "conan仙人指路" <conan_...@hotmail.com> wrote: > Hi Faisal, > > CC-half standard is valuable in evaluating the cut-off of highest > resolution. Sometimes even if I/sigI is close to 1 and completeness is not > as high, if CC-half is still significant, it may be worth incorporate the > extra high-res shell data and extend the resolution. Again, if only the > reliability and unbias are carefully confirmed, and the apparent > significant CC-half is not due to an artifact of some other factors like > ice ring etc. > (Ref: Karplus PA and Diederichs K. 2012 Science 336, 1030-1033 > https://www.pubmed.com/pubmed/22628654) > > It has yet to be appreciated by most population of the crystallography > society, unlike the I/sigI, completeness, Rsym. In particular, Rsym has > gradually less a direct measurement of the data quality and or determinant > of resolution cut-off. > > Best, > Conan > > Hongnan Cao, Ph.D. > Department of Biochemistry > Rice University > > ------------------------------ > Date: Fri, 15 Aug 2014 01:39:48 +0530 > From: faisaltari...@gmail.com > Subject: [ccp4bb] CC-half value ?? > To: CCP4BB@JISCMAIL.AC.UK > > Dear all > > How CC-half value of a data set determines the maximum resolution limit > during data processing ?? Although much we know about the Rsym and I/Isig > values of the highest resolution shell while processing the data, what are > the parameters we need to check related to CC-half values ?? > > -- > Regards > > Faisal > School of Life Sciences > JNU > > ------------------------------ Date: Thu, 14 Aug 2014 15:13:48 -0700 From: Daniel Anderson <d...@mbi.ucla.edu> Subject: Re: dynapro DLS cuvettes Hello, Gloria and everybody, I'm typing most of this reply from memory. When I tried to buy one, my recollection was that it was available from Hellma, but I couldn't (and still can't) find my Hellma paper catalog, and for some reason I did not find the Hellma web site when I wanted to buy a cuvette. I have since learned to spell "Google". I have the starnacells dot com paper catalog in front of me. What you want is almost catalog number 16.12F-Q-1.5/Z15. The Z parameter should probably be closer to 14 than 15mm. That catalog number from Starna is probably the one that I bought some years ago, and here is my recollection of what happened: The cell arrived, and I found that light did not go through unless I pushed it sideways. I measured the old Dynapro cuvette, and it was 12.45x12.45mm. The cell from Starna was 12.25x12.35mm. I returned it and Starna sent me a replacement that was 12.35x12.25mm. When this comedy of rectangular cuvettes tired me I returned the nth cell that they sent me and gave up trying to buy one. One more detail: the above recollections are about a 13,714-year old DynaPro with the microcuvette device added as post-translational modification. It's so old that the serial number is probably negative. I don't know if a more recent instrument has the same cuvette holder geometry. I hope that partial information helps, Dan Gloria Borgstahl wrote: > Does any one know of a source of these cuvettes? > Protein Solution doesn't exist anymore > and Wyatt no longer has these. ------------------------------ End of CCP4BB Digest - 13 Aug 2014 to 14 Aug 2014 (#2014-220) *************************************************************
