[ccp4bb] Senior Postdoctoral position(s) in Structural Biology
We are looking for senior postdoctoral researchers to join an exciting structure-based drug design project funded by the Bill Gates foundation in the Sayers' laboratory to develop inhibitors of a Plasmodium nuclease involved in DNA replication. These posts have arisen from a successful feasibility study also funded by the foundation. For background on the nuclease and our work in this area click here <http://www.sayers.staff.shef.ac.uk/fen/index.html>. One post requires a PDRA with proven experience in protein structure determination by NMR. The application documents for this post can be found here. here. <https://tinyurl.com/2p9aahsc> Documents for the second post (which requires a PDRA with experience in X-ray crystallography ) will be released shortly. This Sheffield University-based project is supported by extensive Medicinal Chemistry, ADME/PK and parasite testing resources from worldwide collaborators arranged by the foundation and represents a truly exciting opportunity to be involved in the fight against malaria. The posts are for up to 16 months in the first instance. The posts are both time sensitive meaning that candidates able to commence quickly will be at an advantage. You will join a group of three other PDRAs working on this project and an MCIF fellow working on a related program in Trypanosomes. The NMR work will be carried out in Prof. Jon Waltho's lab and crystallography is supervised by Dr Pat Baker (both Sheffield). The posts are both based in Sheffield, UK. Depending on experience, we are able to appoint at or near the top end of the scale advertised. Feel free to contact me to discuss. -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk https://www.sheffield.ac.uk/iicd/profiles/sayers <http://www.sheffield.ac.uk/iicd/profiles/sayers> To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
[ccp4bb] Postdoctoral research positions in structural biology
HEADS UP (there will be an official announcement soon) We are looking for two postdoctoral researchers to join an exciting structure-based drug design project funded by the Bill Gates foundation to develop inhibitors of a Plasmodium nuclease involved in DNA replication. One post requires a PDRA with proven experience in protein structure determination by NMR. The other requires a PDRA with experience in X-ray crystallography and protein biochemistry. This Sheffield University based project is supported by extensive Medicinal Chemistry, ADME/PK and parasite testing resources from collaborators arranged by the foundation. The posts are for up to 18 months depending on how soon official advertisements etc can be processed. The posts are both time sensitive. You will join a group of three other PDRAs working on this project and an MCIF fellow working on a related program in Trypanosomes. The NMR work will be carried out in Prof. Jon Waltho's lab and crystallography is supervised by Dr Pat Baker (both Sheffield). The posts are both based in Sheffield, UK. -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk https://www.sheffield.ac.uk/iicd/profiles/sayers <http://www.sheffield.ac.uk/iicd/profiles/sayers> To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
[ccp4bb] Post-doc position in structural biology/drug discovery/design
We wish to appoint a talented and ambitious Research Associate to develop novel approaches to targeting malaria and tuberculosis. Drug resistance is becoming increasingly problematic in malaria and TB, two of the most-deadly diseases in human history. The WHO estimates that there were over half a million cases of drug-resistant TB in 2017. This exciting pilot project is funded by the Bill Gates Foundation for 13 months to investigate the feasibility of developing inhibitors of DNA replication in these globally important pathogens. You will have a Ph.D. (or be close to completion) in a relevant life-sciences subject and experience in X-ray crystallography, structure refinement, protein purification and executing crystallization trials. The successful applicant will conduct world-class research in structure-based drug design to develop inhibitors of microbial flap endonucleases (FENs). FEN enzymes are involved in cellular DNA synthesis and genome damage repair. We have shown that a member of this important class of enzymes contains a novel DNA-binding motif, the helical arch (Al Malki et al, Direct observation of DNA threading in flap endonuclease complexes. 2016, Nature Structural and Molecular Biology, 23, 640-646). You will facilitate production, crystallization and X-ray crystal structure determination of FEN enzymes and their complexes with inhibitors. You will work closely with a second postdoctoral Research Associate carrying out enzyme production and inhibitor assays as well as with chemo- informatics experts. We welcome highly dedicated and enthusiastic candidates with the ability to develop their scientific skills in the direction of rational drug design. You will join a multi-disciplinary team spanning two research groups: The Sayers lab is based within the Dept. of Infection, Immunity and Cardiovascular Disease; and the Baker group is housed within the Dept. of Molecular Biology and Biotechnology. This vibrant team works on FEN mechanism and applications in biotechnology as well as inhibitor discovery in other target organisms. We use site- directed mutagenesis, crystallography and kinetic approaches to determine how these complicated enzymes function in order to design inhibitors in conjunction with virtual and physical screening. The groups are housed within well-equipped laboratories with access to excellent core facilities with state-of-the-art equipment for e.g. biological mass spectrometry, nucleic acid sequencing, X-ray crystallography, liquid handling for high throughput screening, crystallization robotics, plus a range of microscopy facilities, etc. The Sayers group hosts a Marie Curie Individual Fellow and PhD students working on homologous FENs derived from bacteria and viruses. For more details of our FEN research see: www.sayers.staff.shef.ac.uk/fen/index.html -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB=1
[ccp4bb] Urgent: Postdoc in protein crystallography / drug discovery
We wish to appoint to the following post *as soon as possible:* We seek to appoint a Research Associate in Structural Biology to work on the development of inhibitors of bacterial flap endonucleases (FEN) as potential new antimicrobial drugs. This is initially for a 16-month period to develop a new generation of anti-bacterial agents capable of targeting antibiotic resistant bacteria. You will join a team during structure-based drug design to develop inhibitors of essential bacterial enzymes. Your role will be to prepare recombinant proteins, crystallise them and determine their X-ray structures. We welcome highly dedicated and enthusiastic candidates with the ability to develop their computer and wet laboratory skills. You will possess or have submitted a PhD degree in X-ray crystallography of protein molecules and have an interest in applying your expertise to structure-based drug development. Success in this post may lead to an opportunity to continue on the project subject to further funding being obtained. FEN enzymes are involved in DNA replication and repair ( Nature Structural and Molecular Biology, 2016 :640-6. doi: 10.1038/nsmb.3241). We are using site-directed mutagenesis, crystallography and kinetic studies to assist in a structure-based drug design approach. We are housed within well-equipped laboratories with access to excellent core facilities with state-of-the-art equipment for e.g. biological mass spectrometry, Cryo-EM, X-ray crystallography, liquid handling robotics for high throughput screening & crystallization, a range of microscopy facilities, etc. You will join a multidisciplinary team representing a collaboration between The Sheffield Institute for Nucleic Acids (SInfoNiA <http://genome.sheffield.ac.uk/>) and The Flory Institute for Host-pathogen Interactions <http://www.floreyinstitute.com/>. This post is fixed term for 16 months, with a start date of 1st March 2018 (or as soon as possible thereafter). Closing date 5th Feb. Previous applicants need not apply. Formal applications to be made via the UoS web site. https://www.sheffield.ac.uk/jobs. (reference UOS018387). or via: http://www.jobs.ac.uk/job/BHN194/postdoctoral-research-associate-in-structural-biology/ -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
[ccp4bb] Any issues using CCP4 under Mac OSX and High Sierra
Are you Mac Users running CCP4 prods under High Sierra? Sorry if I've missed this in an archive search but as a serial late adopter of new OS releases, I've resisted upgrading until I know things work. BW Jon -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
[ccp4bb] Postdoc position available in structure-based antimicrobial drug development
Job Reference Number: Job Title: Contract Type: Working Pattern: Faculty: Department: Salary: £30,688 - £32,548 per annum Closing Date: 15th Jan. 2018 APPLY VIA Current vacancies link on https://www.sheffield.ac.uk/jobs Search for job reference number UOS017984 Postdoctoral Research Associate in Structural Biology /Structure-based drug design We seek to appoint a Research Associate in Structural Biology to work on the development of inhibitors of bacterial flap endonucleases (FEN) as potential new antimicrobial drugs. This is a n university position for 16-month fixed-term funded by a research contract from an exciting new University of Sheffield spin-out company founded to develop a new generation of anti-bacterial agents capable of targeting antibiotic resistant bacteria. You will conduct world-class research to enable a structure-based drug design approach to develop inhibitors of essential bacterial enzymes. Your role will be to crystallize and determine the X-ray crystal structures of FEN enzymes and to carry out structure-based drug screening/design . You will work closely with a second Research Associate tasked with protein manufacture, inhibitor characterization and development. We welcome highly dedicated and enthusiastic candidates with the ability to develop their scientific skills. You will possess or have submitted a PhD degree in X-ray crystallography of protein molecules and have an interest and ideally experience in in silico drug development. Success in this post may lead to an opportunity to continue on the project subject to further funding being obtained. FEN enzymes are involved in DNA replication and repair (see our recent paper in Nature Structural and Molecular Biology on the mechanism). We are using site-directed mutagenesis, crystallography and kinetic studies to determine how these complicated enzymes function and you will apply this to developing inhibitors in a structure-based approach. The groups are housed within well-equipped laboratories with access to excellent core facilities with state-of-the-art equipment for e.g. biological mass spectrometry, Cryo-EM, X-ray crystallography, liquid handling robotics for high throughput screening & crystallization, a range of microscopy facilities, etc. You will join a multidisciplinary team made up of scientists from the Sayers’ and Baker laboratories from the Department of Infection, Immunity and Cardiovascular Disease, (IICD) and Department of Molecular Biology & Biotechnology (MBB), respectively. This represents a collaboration between two research institutes in Sheffield, namely, The Sheffield Institute for Nucleic Acids (SInfoNiA) and The Flory Institute for Host-pathogen Interactions. You will hold a good honours degree in a relevant subject and a PhD in macromolecular crystallography. This post is fixed term for 16 months, with a start date of 1 February 2018 (or as soon as possible thereafter). -- Professor Jon R Sayers, FRSB Department of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom Tel: +44 (0)114 215 9552 Fax: +44 (0)114 271 1863 Email: j.r.say...@sheffield.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
[ccp4bb] Postdoctoral postion available- Structure-based antimicrobial drug development - UK
*Postdoctoral position at the University of Sheffield, UK* *PDRA in Structure-based antimicrobial drug development* Applications are invited for a Research Associate in Structural Biology (ideally with some knowledge of in silicon drug screening vHTS) with a start date of 1 Jan 2018 or as soon as possible thereafter. This is initially a 16-month fixed-term position funded by a research contract from DeFENition Ltd, an exciting University of Sheffield spin-out company founded to develop a new generation of anti-bacterial agents capable of targeting antibiotic resistant bacteria. The successful applicant will conduct world-class research in structural biology and will work closely with a second Research Associate tasked with protein manufacture and inhibitor characterization*.* *The project will be jointly conducted by the Sayers and Baker groups hosted by the Department of Infection, Immunity and Cardiovascular Disease, (IICD) and Department of Molecular Biology & Biotechnology (MBB), respectively at **the** University of Sheffield, UK.* *IICD is situated within the Medical School and encompasses basic research in molecular cell biology in Respiratory Medicine, Infectious Diseases, Renal Medicine, Dermatology, Cardiovascular science and both biomedical and medical imaging. MBB is located centrally in the University campus adjacent to sister departments of Biomedical Science and Animal and Plant Sciences. Together the biology departments host around 100 academic staff and research fellows and teach 1,500 undergraduate students. The three departments are renowned for cutting edge research and have internationally recognized strengths in evolutionary biology and genetics, cell and developmental biology, stem cell biology, behavior and neuroscience, human health and disease, plant science, microbiology, ecology and environmental biology and structural and quantitative biology. Staff also work very closely with scientists and clinicians across the Science, Engineering and Medical Faculties.* *Baker and Sayers are members of Sheffield’s Florey Institute for Host Pathogen Interactions http://www.floreyinstitute.com <http://www.floreyinstitute.com/> and **Sheffield Institute for Nucleic Acids (SInFoNiA)* http://genome.sheffield.ac.uk. * Together we are developing radical solutions to the global problems of disease and antimicrobial drug resistance. Baker and Sayers were part of Unit of Assessment 3, (Allied Health Professions, Dentistry, Nursing and Pharmacy - Biomedical science) which was placed 1st of 96 UK departments in REF2014.* *Starting salary £30,688 - £32,548 (plus annual increment).* *Please contact me for further information.* -- Best wishes Prof. Jon R Sayers, FRSB Tel: +44 (0) 114 2159552 Email: j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
Re: [ccp4bb] [phenixbb] comfortable OS X level
REFMAC and COOT seem fine on my iMac running 10.12.5 On 7 June 2017 at 17:28, Diana Tomchick <diana.tomch...@utsouthwestern.edu> wrote: > Hahahaha, that was a typo, I meant to write > > 10.12.5 > > Diana > > ** > Diana R. Tomchick > Professor > Departments of Biophysics and Biochemistry > University of Texas Southwestern Medical Center > 5323 Harry Hines Blvd. > Rm. ND10.214A > Dallas, TX 75390-8816 > diana.tomch...@utsouthwestern.edu > (214) 645-6383 (phone) > (214) 645-6353 (fax) > > On Jun 7, 2017, at 11:25 AM, Scott Classen <sclas...@lbl.gov> wrote: > > 10.2 ? > That OS is 15 years old. > > > On Jun 7, 2017, at 8:27 AM, Diana Tomchick <Diana.Tomchick@ > utsouthwestern.edu> wrote: > > > > I’ve not had any problems; the current version is 10.2.5, so it’s pretty > stable now. > > > > Diana > > > > ** > > Diana R. Tomchick > > Professor > > Departments of Biophysics and Biochemistry > > University of Texas Southwestern Medical Center > > 5323 Harry Hines Blvd. > > Rm. ND10.214A > > Dallas, TX 75390-8816 > > diana.tomch...@utsouthwestern.edu > > (214) 645-6383 (phone) > > (214) 645-6353 (fax) > > > > On Jun 7, 2017, at 10:14 AM, Patrick Loll <pat.l...@drexel.edu> wrote: > > > > I’m still running Yosemite on my Macs, both because I’m change-averse > and because folks reported problems with some crystallographic software > upon upgrading the OS. > > > > These reports have now faded into the haze of the past, and so I ask, > have the issues been resolved? Is it safe to move to Sierra? > > > > Thanks as always, > > > > Pat > > > > > --- > > Patrick J. Loll, Ph. D. > > Professor of Biochemistry & Molecular Biology > > Drexel University College of Medicine > > Room 10-102 New College Building > > 245 N. 15th St., Mailstop 497 > > Philadelphia, PA 19102-1192 USA > > > > (215) 762-7706 > > pat.l...@drexelmed.edu > > > > > > ___________ > > phenixbb mailing list > > pheni...@phenix-online.org > > http://phenix-online.org/mailman/listinfo/phenixbb > > Unsubscribe: phenixbb-le...@phenix-online.org > > > > > > > > > > UT Southwestern > > > > > > Medical Center > > > > > > > > The future of medicine, today. > > > > > -- Best wishes Prof. Jon R Sayers, FRSB Tel: +44 (0) 114 2159552 Email: j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
Re: [ccp4bb] Problems with an exonuclease
I missed the Triton - that will be it! On 7 June 2017 at 15:46, Bonsor, Daniel <dbon...@som.umaryland.edu> wrote: > It will either be two things. DNA or residual Triton-X-100. When you say, > cleaned the IBs, do you mean you sonicated the IBs, or just resuspended the > pellet and then centrifuged again? If the latter, try sonication. I wash my > IBs at least 4 times with the following buffers; > > > > 1. 20mM Tris, 500mM NaCl, 1% Triton-X-100, pH 7.5 > > 2. 20mM Tris, 500mM NaCl, 1% Triton-X-100, pH 7.5 > > 3. 10mM Tris, 1M NaCl > > 4. 20mM Tris, 500mM NaCl, pH 7.5 > > > > By resuspension and then sonication. This I find removes DNA and > Triton-X-100. > > > > Also, if the pellet is very large, you may need to increase the number of > washes, volume and length of sonication or split the pellet up. > > > > Other things to try… > > 1. Change the wash salt to KCl and use more, (3M). I was informed > that KCl is a better disrupter of DNA than NaCl (I stand to be corrected if > this is wrong). > > 2. At each wash stage, dissolve a small amount of IBs and measure > the 260/280. The ratio should decrease in the latter washes, if they are > working. > > 3. Does your exonuclease typically contain a divalent metal? You > could try adding EDTA to the wash steps which may help in preventing DNA > stick to your protein. > > > > All the best! > > > > Dan > > > > > > Daniel A Bonsor PhD. > > Sundberg Lab > > Institute of Human Virology > > University of Maryland, Baltimore > > 725 W Lombard Street N370 > > Baltimore > > Maryland > > MD 21201 > > Tel: (410) 706-7457 > > > > > > *From:* CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] *On Behalf Of > *Mohammad > Khan > *Sent:* Wednesday, June 07, 2017 9:37 AM > *To:* CCP4BB@JISCMAIL.AC.UK > *Subject:* [ccp4bb] Problems with an exonuclease > > > > Dear all, > > > > I am working with an exonuclease by refolding it from inclusion bodies > (IBs). I tried various constructs and hosts, but couldn't get it in soluble > form. > > > > I lyse my cells using a cell disruptor and after solubilizing IBs with > urea, I refold the protein by rapid dilution and get an aggregate and > monomer peak of the same on GFC. and have checked CD as well as activity, > both of which are good. > > > > My issues is as follows: > > > > I get a high 260 nm peak while purifying it on GFC. the 260/280 ratio can > reach upto 2. I have tried all means to get rid of watever this > contamination is: cleaned the IBs with 1% Triton X-100, 2 M NaCl, added > Dnase prior to lysis. I have also used methods to remove the DNA from > protein, if that is the contaminating agent. > > I am trying to crystallize the protein with no success so far. > > Moreover, my thermofluor assays give very low fluorescence. I use Sypro > Orange as a fluorophore. > > > > Suprisingly, a point mutation in the active site (His to Arg) gets rid of > the issue of contamination and gives me good thermofluor curves. I purify > the mutant also form IBs. > > > > Can someone suggest what this "contamination" may be? > > > > Thank you for your time. > > > > > -- Best wishes Prof. Jon R Sayers, FRSB Tel: +44 (0) 114 2159552 Email: j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
Re: [ccp4bb] Problems with an exonuclease
Dear Mohammad, If your protein is purified from insoluble material there could be some DNA in there though if it were stoichiometric your 26 would be >> than your 280, as the former has a much higher extinction co-efficient. A ratio of 2 is could be RNA contamination. I'd also check the mass spec of your protein to see if it has any unusual modification - urea is notorious for cause carbamylation of N-terminal amino groups, and of lysine and arginine residues. What that does to UV I'm not sire sure but irrespective of the UV anomaly, I'd always get the beast mass-specced! On 7 June 2017 at 14:36, Mohammad Khan <mohdkhan0...@gmail.com> wrote: > Dear all, > > I am working with an exonuclease by refolding it from inclusion bodies > (IBs). I tried various constructs and hosts, but couldn't get it in soluble > form. > > I lyse my cells using a cell disruptor and after solubilizing IBs with > urea, I refold the protein by rapid dilution and get an aggregate and > monomer peak of the same on GFC. and have checked CD as well as activity, > both of which are good. > > My issues is as follows: > > I get a high 260 nm peak while purifying it on GFC. the 260/280 ratio can > reach upto 2. I have tried all means to get rid of watever this > contamination is: cleaned the IBs with 1% Triton X-100, 2 M NaCl, added > Dnase prior to lysis. I have also used methods to remove the DNA from > protein, if that is the contaminating agent. > I am trying to crystallize the protein with no success so far. > Moreover, my thermofluor assays give very low fluorescence. I use Sypro > Orange as a fluorophore. > > Suprisingly, a point mutation in the active site (His to Arg) gets rid of > the issue of contamination and gives me good thermofluor curves. I purify > the mutant also form IBs. > > Can someone suggest what this "contamination" may be? > > Thank you for your time. > > > -- Best wishes Prof. Jon R Sayers, FRSB Tel: +44 (0) 114 2159552 Email: j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
Re: [ccp4bb] Completely Off-Topic
Following on I read somewhere a while back that potassium conc in E. coli is estimated in the 30-300 mM range (http://book.bionumbers.org/what-are-the-concentrations-of-different-ions-in-cells/ <http://book.bionumbers.org/what-are-the-concentrations-of-different-ions-in-cells/>) . In other more extremophiles it can be higher (Extremophiles <https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4339784/#>. 2015; 19(2): 315–325.)Maybe our default buffers should contain K+ and Glu at such high conc- though not compatible for IEX of course it would appear that such conditions are physiological at least for intracellular bacterial proteins. Prof. Jon R Sayers FRSB Dept. of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom, Tel +44 (0)114 215 9552 Fax +44 (0) 114 271 3892 Email j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers <http://www.sheffield.ac.uk/iicd/profiles/sayers> > On 12 Jan 2017, at 09:13, Reza Khayat <rkha...@ccny.cuny.edu> wrote: > > I don't think this is taught in Biochem101. You didn't miss it. The cytoplasm > is quite viscous, like jello. > > > > Reza Khayat, PhD > Assistant Professor > City College of New York > Department of Chemistry > New York, NY 10031 > > > From: CCP4 bulletin board [CCP4BB@JISCMAIL.AC.UK] on behalf of Tim Gruene > [tim.gru...@psi.ch] > Sent: Thursday, January 12, 2017 3:55 AM > To: CCP4BB@JISCMAIL.AC.UK > Subject: Re: [ccp4bb] Completely Off-Topic > > Dear JPK, > > I was not aware of the absolute numbers, but maybe they are little suprising: > when your tinned food contains 'yeast extract' it is equivalent to monosodium > glutamate, which is commonly used as flavour enhancing agent. > > I am not a chemist to worry about it, but yeast seems to have a fullfilling > life with it. > > Best, > Tim > > On Thursday, January 12, 2017 12:45:03 AM CET Keller, Jacob wrote: >> Dear Crystallographers, >> >> Was anyone else aware that in E coli the intracellular glutamate >> concentration is ~100 mM? Also other cell types (yeast, mammalian) are 10s >> mM. Anything to say about this? I learned of this just recently, and have >> been amazed about it for more than a week. Did I miss this in Biochem 101? >> Does it matter? >> >> JPK >> >> *** >> Jacob Pearson Keller, PhD >> Research Scientist >> HHMI Janelia Research Campus / Looger lab >> Phone: (571)209-4000 x3159 >> Email: kell...@janelia.hhmi.org<mailto:kell...@janelia.hhmi.org> >> *** > > -- > -- > Paul Scherrer Institut > Tim Gruene > - persoenlich - > OFLC/102 > CH-5232 Villigen PSI > phone: +41 (0)56 310 5297 > > GPG Key ID = A46BEE1A Best wishes, Prof. Jon R Sayers FRSB Dept. of Infection, Immunity & Cardiovascular Disease University of Sheffield Medical School Beech Hill Rd Sheffield S10 2RX United Kingdom, Tel +44 (0)114 215 9552 Fax +44 (0) 114 271 3892 Email j.r.say...@shef.ac.uk http://www.sheffield.ac.uk/iicd/profiles/sayers
