[ccp4bb] Crystallographic Postdoctoral Research Position - Berkeley, USA
A postdoctoral research position is available immediately to work on challenging problems in structural biology: Postdoctoral Researcher Job ID: 21615 Division: Physical Biosciences Date Opened: 3/28/2008 This postdoctoral position will study the structure and function of macromolecular complexes and enzymes using X-ray crystallographic methods. This position will be joint between the Center for Protein Folding Machinery (proteinfoldingcenter.org) and the Joint BioEnergy Institute (www.jbei.org). The biological systems to be studied will include: Type-II chaperonins responsible for the refolding of unfolded proteins in archeal and mammalian cells, Glycosyl transferases responsible for the synthesis of hemicellulose in plants, and Novel glycosyl hydrolases that are able to breakdown cellulosic material for biofuels production. The candidate will have experience with using crystallographic methods to study macromolecules; robotic hardware for performing crystallization trials and imaging trays are available. Crystals will be characterized and data collected using the beamline resources of the Berkeley Center for Structural Biology at the Advanced Light Source. Essential: Primary duties and responsibilities will include using robotic hardware to perform screens for crystallization conditions. Optimization of crystallization conditions. Biophysical characterization of protein samples using standard techniques, such as dynamic light scattering. Characterization of crystals using the Berkeley Center for Structural Biology beamlines at the Advanced Light Source. Collection and analysis of diffraction data, model building and structure refinement. Extensive email and verbal interaction with other researchers. Marginal: Use of small angle X-ray scattering methods to analyze macromolecular complexes in solution. Essential: Ph.D. or equivalent in a scientific discipline, preferably structural biology, biology, or chemistry. Demonstrated experience of scientific research using crystallographic methods. Experience with crystallization methods. Solid interpersonal skills and the ability to work in a team environment are critical. Ability to communicate with a broad range of researchers. Marginal: Experience with the use of small angle scattering methods. Familiarity with robotic hardware for crystal growth. NOTE: This is a one year Term appointment with the possibility of renewal under the same terms and conditions, contingent upon continued funding and availability of work. Lawrence Berkeley National Laboratory is a world leader in science and engineering research, with 11 Nobel Prize recipients over the past 75 years, and 59 present members of the National Academy of Sciences. LBNL conducts unclassified research across a wide range of scientific disciplines and hosts four national user facilities. AA/ EEO employer committed to the development of a safe and diverse workforce. Learn more at http://www.lbl.gov. For more information about the Center for Protein Folding Machinery visit: http://proteinfoldingcenter.org/ and the Joint BioEnergy Institute visit: http://www.jbei.org/. For more information about the Berkeley Center for Structural Biology visit: http://bcsb.lbl.gov/ To apply: visit http://cjo.lbl.gov/ and search for the job number 21615. Please see http://cjo.lbl.gov/app_instr.html for details of how to apply. -- Paul Adams Deputy Division Director, Physical Biosciences Division, Lawrence Berkeley Lab Adjunct Professor, Department of Bioengineering, U.C. Berkeley Vice President for Technology, the Joint BioEnergy Institute Head, Berkeley Center for Structural Biology Building 64, Room 248 Tel: 510-486-4225, Fax: 510-486-5909 http://cci.lbl.gov/paul Lawrence Berkeley Laboratory 1 Cyclotron Road BLDG 64R0121 Berkeley, CA 94720, USA. --
Re: [ccp4bb] convenient means to find I/sigma for publications?
It is recorded by SCALA - if you use that data processing procedure. You can still do a run of scala after SCALEPACK or XDS or whatever providing you output integrated, unmerged intensities. You are right though - we need a data analysias tool.. Eleanor James Pauff wrote: Hello all, Silly question, but what is the most convenient means to find the overall I/sigma and the I/sigma for the highest resolution shell in CCP4? At the end of refinement and validation, and after running PROCHECK, I am still using a very convoluted route to obtaining these numbers. Thanks! JMP You rock. That's why Blockbuster's offering you one month of Blockbuster Total Access, No Cost. http://tc.deals.yahoo.com/tc/blockbuster/text5.com
Re: [ccp4bb] libstdc++.so.5
Hi Adam, The symbolic link approach does not work - I hit this problem with another (C++) program. Your pointer about the compat rpm is helpful though - this is probably the most robust solution. I ended up compiling from scratch when I hit a similar problem. Best, Graeme -Original Message- From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On Behalf Of Adam Ralph Sent: 02 April 2008 10:07 To: CCP4BB@JISCMAIL.AC.UK Subject: Re: [ccp4bb] libstdc++.so.5 Dear Shivesh, I believe that Fedora 8 has a more updated version of libstdc++ in /usr/lib. You can install libstdc++.so.5 from compat-libstdc++-33-3.2.3-62 using yum (if you have it). An easier approach would be to make a symbolic link between libstdc++.so.5 and libstdc++.so.6 but there maybe compatibility issues. Has anybody tried this? Adam On Wed, 2 Apr 2008, shivesh kumar wrote: Dear all, We have installed CCP4 6.0.2 in Fedora core 8. While running the program we are getting the following error message- error while loading shared lilbraries libstdc++.so.5, cannot open shared object file: no such file or directory. Please suggest how to get this library file... Thanx in advance shivesh
[ccp4bb] libstdc++.so.5
Dear all, We have installed CCP4 6.0.2 in Fedora core 8. While running the program we are getting the following error message- error while loading shared lilbraries libstdc++.so.5, cannot open shared object file: no such file or directory. Please suggest how to get this library file... Thanx in advance shivesh
Re: [ccp4bb] libstdc++.so.5
Dear Shivesh, I believe that Fedora 8 has a more updated version of libstdc++ in /usr/lib. You can install libstdc++.so.5 from compat-libstdc++-33-3.2.3-62 using yum (if you have it). An easier approach would be to make a symbolic link between libstdc++.so.5 and libstdc++.so.6 but there maybe compatibility issues. Has anybody tried this? Adam On Wed, 2 Apr 2008, shivesh kumar wrote: Dear all, We have installed CCP4 6.0.2 in Fedora core 8. While running the program we are getting the following error message- error while loading shared lilbraries libstdc++.so.5, cannot open shared object file: no such file or directory. Please suggest how to get this library file... Thanx in advance shivesh
[ccp4bb] inclusion body
Dear all, Sorry for the off-topic question... What can be done to avoid a protein going inside inclusion body.The gene is cloned in pET30a with C-ter his tag and expressed in BL21-DE3 from 37 to 18C for 3-4 hr with .5mM of IPTG,it is going to inclusion body.All suggestions are welcome. Thanx in advance. Shivesh
[ccp4bb] a question about CNS composite omit map
Dear all, Sorry this might be another naive, non-ccp4 question~ I was trying to make a composite omit map with CNS, but during torsion angle dynamics, it always reports an argument out of range error like the following: -- step= 5 at 0.02000 ps - | E(kin)+E(total)=52920.147 E(kin)=234.290 temperature=200.000| | Etotal =52685.857 grad(E)=17.535 E(BOND)=79.376 E(ANGL)=566.763| | E(DIHE)=1157.267 E(IMPR)=122.802E(VDW )=2908.858 E(PVDW)=67.125 | | E(HARM)=3.348 E(XREF)=47780.318| --- TORMD: velocity rescaling (VSCAle) enabled -- Torsion Angle Dynamics - WARNING: Velocities taken from last torsion angle dynamics step. --- TORMD3: number of degrees of freedom=1179 -- Initial Conditions - | E(kin)+E(total)=52765.760 E(kin)=175.717 temperature=150.000| | Etotal =52590.043 grad(E)=17.162 E(BOND)=79.634 E(ANGL)=567.386| | E(DIHE)=1158.107 E(IMPR)=122.945E(VDW )=2897.021 E(PVDW)=66.611 | | E(HARM)=3.382 E(XREF)=47694.956| --- NBONDS: found80621 intra-atom interactions NBONDS: found 3240 symmetry-atom interactions %CHEVAL error encountered: argument out of range (CNS is in mode: SET ABORT=NORMal END) * ABORT mode will terminate program execution. * I have tried to increase the Torsion angle MD parameters, but while that solved the problem for one other similar structure (a mutant), it doesn't work for this structure I am talking about. I have two other similar structures with similar resolution (around 2.1A), R/Rfree (0.22/0.24) values and only differ by a couple of residues, and composite_omit_map was fine. Could anyone explain to me what went wrong during these torsion angle dynamics? How could I solve such problem? Thank you very much! Best, Melody
Re: [ccp4bb] inclusion body
Lower temperature, use chaperones (e.g. TAKARA set), refolding? Quoting shivesh kumar [EMAIL PROTECTED]: Dear all, Sorry for the off-topic question... What can be done to avoid a protein going inside inclusion body.The gene is cloned in pET30a with C-ter his tag and expressed in BL21-DE3 from 37 to 18C for 3-4 hr with .5mM of IPTG,it is going to inclusion body.All suggestions are welcome. Thanx in advance. Shivesh
[ccp4bb] Inverse 3D profile/threading
I am looking for software or a server to run the 3D-1D profile search in reverse: that is I have a new structure (not in yet deposited in PDB) and I want to see what sequences might fit well to this 3D structure. Can someone point me in the right direction? -jason
Re: [ccp4bb] inclusion body
Also worth trying a lower IPTG level ~ 0.1mM and or different media, e.g. TB, SOC or m9 instead of LB, it's all a bit random but sometimes these things can make a difference. Adding 3% EtOH on induction worked for me once, it's supposed to shock the cells and stimulate chaperone production, I was surprised I must say. Funny old world.. Giles Robertson D.Phil. [EMAIL PROTECTED] Tel: 02076316813 School of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1E 7HX. On 2 Apr 2008, at 12:19, Brenda Patterson wrote: Lower temperature, use chaperones (e.g. TAKARA set), refolding? Quoting shivesh kumar [EMAIL PROTECTED]: Dear all, Sorry for the off-topic question... What can be done to avoid a protein going inside inclusion body.The gene is cloned in pET30a with C-ter his tag and expressed in BL21-DE3 from 37 to 18C for 3-4 hr with .5mM of IPTG,it is going to inclusion body.All suggestions are welcome. Thanx in advance. Shivesh
Re: [ccp4bb] Co-expression plasmids
I do use the Duet vectors extensively and they work just fine. I have trouble with my protein complex, but that is solely related to my proteins. My lab mate has used these vectors very successfully. I have been using pRSF-Duet and pETDuet1 more than pCDFDuet1 or pACYCDuet1 for no specific reason except for a slight preference for the antibiotics. I avoid pACYCDuet1 (Cam resistance) since a lot of expression cells I use have plasmids with Cam resistance. Also, I recently heard about the chaperone co-expression from Takara and folks claim that this system works well. Also, some folks recommend pCOLD vectors (Takara). Might be worth looking into if you are shopping anyway. I don't think these are for co-expression but it is just as easy to stitch in a T7 promoter and RBS to incorporate additional genes. Hope that helps. Raji -Included Message-- Date: 2-apr-2008 09:56:09 -0400 From: Mark J. van Raaij [EMAIL PROTECTED] To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] Co-expression plasmids Dear All, Anyone have experience with the NovaGen Duet co-expression vectors? Or can recommend others? http://www.emdbiosciences.com/html/NVG/Duet_Spot.html Greetings, Mark Mark J. van Raaij Dpto de Bioqu#237;mica, Facultad de Farmacia Universidad de Santiago 15782 Santiago de Compostela Spain http://web.usc.es/~vanraaij/ -End of Included Message--
[ccp4bb] twinned?
Hi all, The data I am working on has a strong translation vector. The space group is C2221 and resolution is 2.3 angstrom. There are two molecules per AU with a pseudo-2-fold axis. On the cumulative intensity distribution plot, the theor and obser curves totally do not overlap. I did detect_twinning from CNS, and there is the result: |I|^2/(|I|)^2 = 3.2236 (2.0 for untwinned, 1.5 for twinned) (|F|)^2/|F|^2 = 0.6937 (0.785 for untwinned, 0.865 for twinned) Does the result mean my data is not twinned? Any suggestion will be highly appreciated. Thank you! The information transmitted in this electronic communication is intended only for the person or entity to whom it is addressed and may contain confidential and/or privileged material. Any review, retransmission, dissemination or other use of or taking of any action in reliance upon this information by persons or entities other than the intended recipient is prohibited. If you received this information in error, please contact the Compliance HelpLine at 800-856-1983 and properly dispose of this information.
[ccp4bb] difference betwen blue confocal max-flux and osmic confocal max-flux
Dear CCP4 Members, Apologise for a non-ccp4 question. Could anybody give the difference between blue confocal max-flux optics (supplied by Rigaku) and osmic confocal max-flux optics (supplied by ?). Are they use same technology (i.e. max-flux) or different? Thanking you Sincerely Karthik
Re: [ccp4bb] twinned?
Hi Qiang, A normal data set has a unimodal intensity distribution with a predictable shape. When there is twinning the distribution remains unimodal but becomes sharper and this is picked up in the twinning analysis. When there is pseudo-translational symmetry, as you indicate you have, then the intensity distribution becomes bimodal with one set of reflections systematically strengthened and another systematically weakened. This makes the whole distribution broader, just the opposite of what twinning does, and therefore shows up as negative twinning in the analysis. Bart Qiang Chen wrote: Hi all, The data I am working on has a strong translation vector. The space group is C2221 and resolution is 2.3 angstrom. There are two molecules per AU with a pseudo-2-fold axis. On the cumulative intensity distribution plot, the theor and obser curves totally do not overlap. I did detect_twinning from CNS, and there is the result: |I|^2/(|I|)^2 = 3.2236 (2.0 for untwinned, 1.5 for twinned) (|F|)^2/|F|^2 = 0.6937 (0.785 for untwinned, 0.865 for twinned) Does the result mean my data is not twinned? Any suggestion will be highly appreciated. Thank you! The information transmitted in this electronic communication is intended only for the person or entity to whom it is addressed and may contain confidential and/or privileged material. Any review, retransmission, dissemination or other use of or taking of any action in reliance upon this information by persons or entities other than the intended recipient is prohibited. If you received this information in error, please contact the Compliance HelpLine at 800-856-1983 and properly dispose of this information. -- == Bart Hazes (Assistant Professor) Dept. of Medical Microbiology Immunology University of Alberta 1-15 Medical Sciences Building Edmonton, Alberta Canada, T6G 2H7 phone: 1-780-492-0042 fax:1-780-492-7521 ==
Re: [ccp4bb] Inverse 3D profile/threading
Hi Jason, RosettaDesign server will do just that: http://rosettadesign.med.unc.edu/ You can specify that certain residues remain unchanged (say active site), that they fall into defined physico-chemical categories (polar, hyrophobic, etc), or let the server change all residues into whatever is compatible with your original structure. If you want a stand-alone version of Rosetta: http://depts.washington.edu/ventures/UW_Technology/Express_Licenses/Rosetta/ At 06:45 AM 4/2/2008, Jason Greenwald wrote: I am looking for software or a server to run the 3D-1D profile search in reverse: that is I have a new structure (not in yet deposited in PDB) and I want to see what sequences might fit well to this 3D structure. Can someone point me in the right direction? -jason == | Mensur Dlakic, PhD| Tel: (406) 994-6576| | Department of Microbiology| Fax: (406) 994-4926| | Montana State University | Lab: (406) 994-6237| | 109 Lewis Hall, P.O. Box 173520 | http://myprofile.cos.com/mensur| | Bozeman, MT 59717-3520| E-mail: [EMAIL PROTECTED]| ==
Re: [ccp4bb] Co-expression plasmids
We have had good experience with the awfully simple minded approach of using two pET vectors with different antibiotic resistance. Its the easiest thing to do, and it often works ... Apologies for the shameless plugin, since there are many good papers on the subject, but you can read some hints and case studies at: http://scripts.iucr.org/cgi-bin/paper?S0907444906031003 (its Open Access) A. On 2 Apr 2008, at 19:39, P Hubbard wrote: Hi, If you are expressing just two proteins, you could try a single pET vector with a pCDF vector. The only reason I'm suggesting this is that I had trouble with pET-Duet, but doing each one separately worked first time (plasmid size issue?). I used pET24-a and pCDF-1b - so I had one construct untagged, and the other with a cleavable His-tag. Cheers AGS Date: Wed, 2 Apr 2008 15:55:27 +0200 From: [EMAIL PROTECTED] Subject: [ccp4bb] Co-expression plasmids To: CCP4BB@JISCMAIL.AC.UK Dear All, Anyone have experience with the NovaGen Duet co-expression vectors? Or can recommend others? http://www.emdbiosciences.com/html/NVG/Duet_Spot.html Greetings, Mark Mark J. van Raaij Dpto de Bioquímica, Facultad de Farmacia Universidad de Santiago 15782 Santiago de Compostela Spain http://web.usc.es/~vanraaij/ Get in touch in an instant. Get Windows Live Messenger now.
Re: [ccp4bb] Co-expression plasmids
I thought only I was having trouble with cloning into pETDuet1. But just to add to what someone just said Yes, I had hell with trying to get one of my ~2kb fragments into pETDuet1 (5.4kb). Could be a combination of vector size and insert size.. Who knows! Sometimes, I do what Tasos says: Transform two plasmids into cells, either sequentially or co-transform. I just play down the amount of each DNA to be used. Raji -Included Message-- Date: 2-apr-2008 09:56:09 -0400 From: Mark J. van Raaij [EMAIL PROTECTED] To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] Co-expression plasmids Dear All, Anyone have experience with the NovaGen Duet co-expression vectors? Or can recommend others? http://www.emdbiosciences.com/html/NVG/Duet_Spot.html Greetings, Mark Mark J. van Raaij Dpto de Bioqu#237;mica, Facultad de Farmacia Universidad de Santiago 15782 Santiago de Compostela Spain http://web.usc.es/~vanraaij/ -End of Included Message--
Re: [ccp4bb] Co-expression plasmids
Just to explain to people who've never had to do co-expression - if I remember correctly, conventional wisdom states that you can't have two different vectors with the same origin of replication in the same host (maybe someone might know more details as to why). However, as pointed out, it can be made to work. Alas, not in my case! CC: CCP4BB@JISCMAIL.AC.UK From: [EMAIL PROTECTED] Subject: Re: [ccp4bb] Co-expression plasmids Date: Wed, 2 Apr 2008 19:59:09 +0200 To: [EMAIL PROTECTED] We have had good experience with the awfully simple minded approach of using two pET vectors with different antibiotic resistance.Its the easiest thing to do, and it often works ... Apologies for the shameless plugin, since there are many good papers on the subject, but you can read some hints and case studies at: http://scripts.iucr.org/cgi-bin/paper?S0907444906031003 (its Open Access) A. On 2 Apr 2008, at 19:39, P Hubbard wrote:Hi, If you are expressing just two proteins, you could try a single pET vector with a pCDF vector. The only reason I'm suggesting this is that I had trouble with pET-Duet, but doing each one separately worked first time (plasmid size issue?). I used pET24-a and pCDF-1b - so I had one construct untagged, and the other with a cleavable His-tag. Cheers AGS Date: Wed, 2 Apr 2008 15:55:27 +0200 From: [EMAIL PROTECTED] Subject: [ccp4bb] Co-expression plasmids To: CCP4BB@JISCMAIL.AC.UK Dear All,Anyone have experience with the NovaGen Duet co-expression vectors? Or can recommend others? http://www.emdbiosciences.com/html/NVG/Duet_Spot.html Greetings,MarkMark J. van RaaijDpto de Bioquímica, Facultad de FarmaciaUniversidad de Santiago15782 Santiago de CompostelaSpainhttp://web.usc.es/~vanraaij/ Get in touch in an instant. Get Windows Live Messenger now. _ Get in touch in an instant. Get Windows Live Messenger now. http://www.windowslive.com/messenger/overview.html?ocid=TXT_TAGLM_WL_Refresh_getintouch_042008
Re: [ccp4bb] Co-expression plasmids
Hi Mark, Proper co-expression in trans requires that you use plasmids each with different origins of replication and antibiotic markers, such as p15 + Kan and ColE1 + Amp. I think the pET vectors of the DUET system use these two origins (p15 and ColE1). This ensures much more efficient dual transformation and proper plasmid stability over time. The two backbone constructions above are used in a variety of pET vectors, so if you look for this detail, you can co-transform and co-express from many available plasmids and customize as you like. Suppliers will tell you the origins that are used in each of the plasmids they sell. Cheers, Brian = Brian L. Mark, MSc, PhD Assistant Professor Department of Microbiology Room 418, Buller Building University of Manitoba Winnipeg, Manitoba CANADA R3T 2N2 Phone (204) 480-1430 Fax (204) 474-7603 Web: http://www.umanitoba.ca/science/microbiology/staff/mark/ On 2-Apr-08, at 8:55 AM, Mark J. van Raaij wrote: Dear All, Anyone have experience with the NovaGen Duet co-expression vectors? Or can recommend others? http://www.emdbiosciences.com/html/NVG/Duet_Spot.html Greetings, Mark Mark J. van Raaij Dpto de Bioquímica, Facultad de Farmacia Universidad de Santiago 15782 Santiago de Compostela Spain http://web.usc.es/~vanraaij/
[ccp4bb] 3D model in glass
Dear all, Anyone know about how to transfer a 3D image (ligand + protein surface) into a format that would be compatible for 3D laser engraving in plexiglass. I am aware of a few cies that can provide the final product (see below) but we are looking for file format information Luminorum (UK) Crystal Protein (California) Molecular dimension (UK and USA) Any others? Thanks, René Rene Coulombe Research Scientist, Chemistry Structural Research Group Boehringer Ingelheim (Canada) Ltd; RD 2100, rue Cunard, Laval (Quebec) Canada H7S 2G5 [EMAIL PROTECTED] tel 450 682-4640 fax 450 682-4642
[ccp4bb] Mg++ binding to N7 of G
Howdie folks: I've got what appears to be an inner-sphere interaction between Mg++ and the N7 of a G. The mode of binding is the same as what is observed at this site for Mn++, confirmed with anomalous data. Our resolution is 1.6 Å, so I am reasonably confident this is right. However, my chemist's viewpoint is that Mg++ is too hard and N is too soft for this to happen. I looked in a database called http://merna.lbl.gov for Mg++ binding sites, and a bunch pop up for inner-sphere N7 interactions with Mg++. However, if I restrict the search to structures having 1.8 Å resolution or better, the number goes to zero. Since Mg++ has the same number of electrons as water and no useful absorbance, it seems assigning them based on hydration geometry and bond distances is the only hope. Does anyone have anything more definitive I can refer to? Thanks. Bill Scott
Re: [ccp4bb] Mg++ binding to N7 of G
Sorry, I should have been less cryptic: On Apr 2, 2008, at 2:13 PM, Jacob Keller wrote: Forgive the naive questions: To what do the terms hard and soft refer here? In inorganic chemistry, hard refers to bonding where the Coulomb potential dominates, and soft where orbital terms dominate. If one partner prefers electrostatic interactions and the other more covalent- like interactions, the interaction is less probable. So Mg++ likes oxygen, Mn++ likes Nitrogen. And G, I assume, is glycine, Guanine but what is N7? Purine numbering... JPK *** Jacob Pearson Keller Northwestern University Medical Scientist Training Program Dallos Laboratory F. Searle 1-240 2240 Campus Drive Evanston IL 60208 lab: 847.491.2438 cel: 773.608.9185 email: [EMAIL PROTECTED] *** - Original Message - From: William G. Scott [EMAIL PROTECTED] To: CCP4BB@JISCMAIL.AC.UK Sent: Wednesday, April 02, 2008 3:58 PM Subject: [ccp4bb] Mg++ binding to N7 of G Howdie folks: I've got what appears to be an inner-sphere interaction between Mg++ and the N7 of a G. The mode of binding is the same as what is observed at this site for Mn++, confirmed with anomalous data. Our resolution is 1.6 Å, so I am reasonably confident this is right. However, my chemist's viewpoint is that Mg++ is too hard and N is too soft for this to happen. I looked in a database called http://merna.lbl.gov for Mg++ binding sites, and a bunch pop up for inner-sphere N7 interactions with Mg++. However, if I restrict the search to structures having 1.8 Å resolution or better, the number goes to zero. Since Mg++ has the same number of electrons as water and no useful absorbance, it seems assigning them based on hydration geometry and bond distances is the only hope. Does anyone have anything more definitive I can refer to? Thanks. Bill Scott
Re: [ccp4bb] 3D model in glass
Dear Rene I have used a company called Imaage in Australia for engraving proteins in glass blocks. Their web address is http://www.imaage.com.au/ I send them VRML output from MOLSCRIPT and that usually works fine. You need to generate the image in a single color (black), though you can use a second color if you want them to map that to a different dot density of laser etching. cheers Mike Lawrence, PhD WEHI Principal Research Fellow Division of Structural Biology Walter and Eliza Hall Institute of Medical Research 1G Royal Parade, Parkville Victoria 3050, AUSTRALIA Tel. 61-3-9345-2693 Fax 61-3-9345-2686 Email: [EMAIL PROTECTED] On 03/04/2008, at 6:29 AM, [EMAIL PROTECTED] wrote: Dear all, Anyone know about how to transfer a 3D image (ligand + protein surface) into a format that would be compatible for 3D laser engraving in plexiglass. I am aware of a few cies that can provide the final product (see below) but we are looking for file format information Luminorum (UK) Crystal Protein (California) Molecular dimension (UK and USA) Any others? Thanks, René Rene Coulombe Research Scientist, Chemistry Structural Research Group Boehringer Ingelheim (Canada) Ltd; RD 2100, rue Cunard, Laval (Quebec) Canada H7S 2G5 [EMAIL PROTECTED] tel 450 682-4640 fax 450 682-4642
[ccp4bb] Production of recombinant membrane protein complex in E. coli
Dear all, Dose anyone have experience about the production of recombinant membrane protein complex in E. coli? All suggestions are welcome. Thanks in advance. Yi-Wei Chang Institute of Molecular Biology Academia Sinica, Taiwan
