[ccp4bb] postdoctoral position in structural neurobiology at Yale University
A postdoctoral position at Yale University School of Medicine is available immediately for highly motivated, creative individuals with a strong interest in the structure, function, and pharmacology of signaling proteins implicated in neurological and neuropsychiatric diseases. We are presently focusing our efforts on central nervous system transporters using a combination of steady-state kinetics, radioligand binding, X-ray crystallography, nanodisc technology, hydrogen-deuterium exchange mass spectrometry (HDX-MS), and other complementary biochemical/biophysical techniques. The laboratory is located in renovated space in the Department of Cellular and Molecular Physiology in a highly collaborative environment. We have state-of-the-art facilities for expression, purification, functional characterization, crystallization, and structure determination of membrane/glyco proteins. We have regular access to Mosquito and Art Robbins Gryphon LCP (lipidic cubic phase) crystallization robots, Formulatrix imager with UV detection, in-house X-ray diffractometer, synchrotron beamlines, LINUX workstations, and biophysical instruments. These include a CD spectrophotometer, Biacore, small-volume isothermal titration calorimeter (NanoITC), stopped flow fluorometer, hydrogen-deuterium exchange mass spectrometer, and laser light scattering coupled in-line to SEC, refractive index, and ultraviolet absorption. Candidates must hold (or soon expect to hold) a recent Ph.D. (less than 1 year) in biochemistry, biophysics, or a related field and have a strong publication record. A strong background in recombinant DNA methods, protein expression, purification, and biochemical/biophysical characterization, crystallization, and structure determination is required. Familiarity with membrane proteins, insect/mammalian cell expression, membrane protein reconstitution, and flux assays is preferred. He/she must be capable of working independently and as part of a collaborative team. An ability to troubleshoot experimental difficulties is a necessity. The candidate must have an excellent command of oral and written English. In addition to compiling and analyzing data, he/she will be responsible for providing some help in preparation of materials for publications and grant proposals. Those able to write and submit successful fellowship applications will have a significant competitive advantage. Applicants should send a CV, along with a summary of previous research experience and interests, and arrange to have 3 reference letters sent to Satinder K. Singh via e-mail at satinder.k.si...@yale.edumailto:satinder.k.si...@yale.edu For more information, please contact me via e-mail. Additional contact information is given below: Satinder K. Singh, Ph.D. Assistant Professor of Cellular and Molecular Physiology Yale University School of Medicine 333 Cedar Street, SHM B147 Lab room # SHM BE11/17 P.O. Box 208026 New Haven, CT 06520-8026 Office #: 203-737-4861 Fax #: 203-785-4951 Cell #: 612-961-4948 E-mail: satinder.k.si...@yale.edumailto:satinder.k.si...@yale.edu Website: http://physiology.yale.edu/people/satinder_k_singh-3.profile Thank you. Kind regards, Satinder
[ccp4bb] Postdoctoral Position in Structural Biology of Chromatin Regulators in Grenoble
Postdoctoral Position in Structural Biology of Chromatin Regulators in Grenoble A 2-year post-doctoral position is available in the newly established group of Jan Kadlec at the Institut de Biologie Structurale (IBS) in Grenoble, France to study the structure and function of chromatin regulatory complexes. The main focus will be on MOF histone acetyltransferase containing complexes. We use an interdisciplinary approach combining structural biology (primarily X-ray crystallography), biochemistry, cell biology and genetics (see Kadlec et al, NSMB 18:142-149 (2011), Hallacli et al, Mol. Cell**48:587-600 (2012), Dias et al, Genes Dev. 28: 929-942 (2014)). The IBS is a member of the Partnership for Structural Biology (www.psb-grenoble.eu http://www.psb-grenoble.eu) providing access to integrated state-of-the-art structural biology technologies, including ESRF synchrotron X-ray beamlines for MX and SAXS, cryo-EM/tomography and NMR as well as biophysics, confocal microscopy and high-throughput crystallization platforms. The successful candidate will be highly motivated and have recently acquired a PhD in the field of biochemistry/structural biology. Skills in complex sample preparation methods (protein expression and purification) are required and experience in protein crystallography would be an advantage. Interested applicants should directly contact Jan Kadlec (kad...@embl.fr mailto:kad...@embl.fr).
[ccp4bb] Announcement - NSLS-II Early-Science Workshop for NIH-funded beamlines
Sent on behalf of the Workshop Organizing Committee The NIH-funded ABBIX structural biology beamlines at the NSLS-II are approaching completion, delivering two crystallography and one scattering beamline for biological sciences. The performance of these beamlines will present opportunities previously unattainable at synchrotron light sources, creating challenges for data collection and scientific discovery. The beamlines will provide a photon-beam flux density at least five orders of magnitude greater than that achievable at the NSLS, and orders of magnitude greater than that achievable today at any synchrotron light source. Participation in the first science undertaken at these beamlines represents a unique opportunity for scientists to help deliver on their potential. We are organizing a workshop at BNL, to occur on Jan. 28-29, 2015, to help define and develop further the priorities for the scientific commissioning of these beamlines and their entry into routine operation. Interested participants will be able to present and discuss their vision for the early science case for each beamline, thereby helping to shape the international scene for structural biology. Find workshop information at http://workshops.ps.bnl.gov/?w=ABBIXJan2015, including a draft agenda and an opportunity to register and submit an abstract.
[ccp4bb] unknown densities
Hi all, We crystallised a small GTPase expressed in E. Coli and found some densities in GDP/GTP binding site. We didn’t add any GDP/GTP or GDP/GPD homologues during protein expression, purification and crystallisation. The resolution is not high, we couldn’t tell what it is. Is there any method to detect what it is? Thanks! Best wishes! yamei Yamei Yu State Key Laboratory of Biotherapy／Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan University,Chengdu,610041, P.R.China Tel: 15882013485 Email: ymyux...@gmail.com ymyux...@163.com yamei...@scu.edu.cn
Re: [ccp4bb] unknown densities
This is where it’s customary to include a small image or two (or better, a link thereto) which shows the density, and the masters here can tell you there best guesses—seems to be a bit of a parlour game. Also include info on what is in the crystallization condition and protein buffer if you dare. FYI, sometimes native nucleotides can make it through protein purifications if binding is tight. JPK From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Yamei Yu Sent: Monday, December 08, 2014 10:15 PM To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] unknown densities Hi all, We crystallised a small GTPase expressed in E. Coli and found some densities in GDP/GTP binding site. We didn’t add any GDP/GTP or GDP/GPD homologues during protein expression, purification and crystallisation. The resolution is not high, we couldn’t tell what it is. Is there any method to detect what it is? Thanks! Best wishes! yamei Yamei Yu State Key Laboratory of Biotherapy／Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan University,Chengdu,610041, P.R.China Tel: 15882013485 Email: ymyux...@gmail.commailto:ymyux...@gmail.com ymyux...@163.commailto:ymyux...@163.com yamei...@scu.edu.cnmailto:yamei...@scu.edu.cn
[ccp4bb] MR_ROSETTA
Hi All; Could some body explain why I am getting the error message when running MR-Rosetta. Message is Sorry cannot locate a binary starting with mr_protocol.default' in the directory /home/phenix/rosetta_2014.34.57213_bundle/main/source/bin I just download it and locate it in the preferences, wizard and then path to Rosetta. Thanks Bashir -- Muhammad Bashir Khan ** Department of Biochemistry University of Alberta, Canada Canada
Re: [ccp4bb] unknown densities
On Mon, Dec 8, 2014 at 7:24 PM, Keller, Jacob kell...@janelia.hhmi.org wrote: FYI, sometimes native nucleotides can make it through protein purifications if binding is tight. This is especially true for G-proteins, since tight binding to GDP is an essential part of their function. I don't know what to expect from E. coli proteins, but human Ras co-purifies with GDP at close to 1:1. At low resolution, it might be easiest to superimpose the closest nucleotide-bound homolog and see how well the density aligns with the nucleotide. -Nat
[ccp4bb] Refmac5: C-terminal amidation parameters
Dear all, refinement of my protein structure involves a C-terminal amide. Looking through the monomer/link library files mon_lib_list.cif and mon_lib_ind.cif I could not identify a modification or link suitable for amide restraints. I know I could construct a proper .cif myself, however I am baffled since it seems like a common enough modification to be in a standard library. Is there an amide restraint definition in the standard library that I am overlooking? I am using _lib_version 5.41. Regards Markus
