[ccp4bb] Diamond Light Source MX Bag training 25-26 February
Dear all, Diamond Light Source will be holding the next training day for MX BAG Users on Wednesday 25th February and Thursday 26th February 2015. The aim is to provide MX users with sufficient training to be able to operate any of the Diamond MX beamlines efficiently and to get the most benefit from their beamtime. The training will involve hands-on sessions on the suite of five operational MX beamlines (http://www.diamond.ac.uk/mx-home/) as well as offline software sessions. Sessions include: 25th February, afternoon session: Hands on software: Tutorial sessions: * CCP4: structure solution and model building with CCP4 (CCP4 team) * Manual processing with iMosflm (Harry Powell) * Multi crystal analysis / BLEND (Pierre Aller and Richard Gildea) * Processing with the new Dials software for expert users only (Dials team) 26th February, day session on MX beamlines: * MX software: automation in data analysis * Mini-Kappa goniometry / Anomalous data collection * Sample humidity control (HC1) * I24 new end station * In-situ diffraction * Experiment database: new ISPyB interface Registration is free-of-charge with lunch provided on the 25th and 26th February, and accommodation and dinner for the night of the 25th February. Travelling expenses within the UK will also be provided. The training is targeted at all users, and is not limited to students and post docs. It is essential that each BAG sends at least one representative per calendar year. Registration Places are limited to 25 participants. The registration deadline is on the 13th February. Registration is now openhttp://www.diamond.ac.uk/Home/Events/2014/MX-Bag-Training.html Best regards, Pierre Pierre Aller, Ph.D. Senior Support Scientist Diamond Light Source Ltd., Diamond House Harwell Science Innovation Campus Didcot, Oxfordshire OX11 0DE +44 (0) 1235 778183 pierre.al...@diamond.ac.uk -- This e-mail and any attachments may contain confidential, copyright and or privileged material, and are for the use of the intended addressee only. If you are not the intended addressee or an authorised recipient of the addressee please notify us of receipt by returning the e-mail and do not use, copy, retain, distribute or disclose the information in or attached to the e-mail. Any opinions expressed within this e-mail are those of the individual and not necessarily of Diamond Light Source Ltd. Diamond Light Source Ltd. cannot guarantee that this e-mail or any attachments are free from viruses and we cannot accept liability for any damage which you may sustain as a result of software viruses which may be transmitted in or with the message. Diamond Light Source Limited (company no. 4375679). Registered in England and Wales with its registered office at Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, United Kingdom
[ccp4bb] EMBO Practical Course on HTP Methods for Protein Production and Crystallization
EMBO Practical Course on HTP Methods for Protein Production and Crystallization Marseille, France, 29 June to 8 July 2015 Deadline for application: 7 April 2015 Dear Colleagues, I am glad to announce the EMBO Practical Course on High Throughput methods for protein production and crystallization hosted at the laboratory AFMB in Marseille, France, from 29 June to 8 July 2015. We would be glad if you could inform your colleagues and students about the course. The course is intended for PhD students and young researchers using highthroughput methods for expression and crystallization of soluble proteins. The goal is to provide participants with the current knowledge in the use of the most innovative methods in the field. For more information and for application, please visit: http://events.embo.org/15-htp-protein/ Best wishes, Gerlind Sulzenbacher, on behalf of the Organizers -- Gerlind Sulzenbacher Architecture et Fonction des Macromolécules Biologiques UMR7257 CNRS, Aix-Marseille Université Case 932 163 Avenue de Luminy 13288 Marseille cedex 9 France Tel +33 491 82 55 66 Fax +33 491 26 67 20 E-mail: gerlind.sulzenbac...@afmb.univ-mrs.fr
[ccp4bb] Faculty position at all levels in structural biology at Stony Brook University, New York
We are recruiting for the above position. More details and the application can be found at https://academicjobsonline.org/ajo/jobs/5289 Stony Brook University Department of Pharmacological Sciences *Tenure-Track Structural Biology / Imaging Faculty Position in Conjunction with the Interdisciplinary Biomolecular Imaging Cluster Hiring Initiative* The Department of Pharmacological Sciences ( http://www.pharm.stonybrook.edu/faculty_research/overview) at Stony Brook University seeks applications for a tenure-track faculty position at the level of Assistant, Associate, or Full Professor. Candidates must have an M.D. and/or Ph.D., at least two years of postgraduate research experience, and an outstanding record of research accomplishment. This search is intended to recruit investigators with translational research programs that make use of NMR, Cryo-EM, or positron emission tomography (PET) coupled with radiotracer synthesis approaches to pursue fundamental questions relevant to health-connected fields such as cancer, neuroscience, metabolism, and infectious disease. Senior candidates should also have a record of success with extramural funding and training of students and/or fellows. Applicants must be eligible for a faculty appointment in accordance with the criteria established by the School of Medicine (Criteria for Appointment, Promotion and Tenure.) The Department has pre-doctoral and MSTP training grants, a broad infrastructure for research investigation, and newly renovated lab space housing structural biologists with expertise in NMR and x-ray crystallography. Additional structural biologists and PET imagers are found in the Departments of Biochemistry, Physiology, Chemistry, and Microbiology. With the on-going NYSUNY 2020 Challenge Grant awarded to the University and the recent and largest gift ever to public higher education in the State of New York, Stony Brook University is embarking on a transformational expansion of the biomedical research enterprise. Diverse opportunities for collaborative research on campus include the Cancer Center, the Laufer Center for Physical and Quantitative Biology, the Center for Structural Biology, the Institute for Chemical Biology and Drug Discovery, and the interactive Computer Science and Applied Mathematics Departments. Imaging biological molecules is key to understanding their function, providing a starting point for rational drug design and protein engineering. Stony Brook University is becoming a leader in biomolecular imaging through its newly-upgraded high-field NMR facilities including Bruker 700MHz and 850 MHz instruments with cryogenic probes, a strong program in computational structural and physical biology, world-class computational resources, facilities for radiotracer synthesis and human imaging, and proximity to the new third-generation synchrotron facility at Brookhaven National Lab (NSLS-II). The Biomolecular Imaging Cluster has already recruited junior faculty with expertise in super-resolution microscopy and x-ray crystallography. Stony Brook University, home to many highly-ranked graduate research programs, is located 60 miles from New York City on Long Island's scenic North Shore. Our 1,100-acre campus has more than 24,000 undergraduate, graduate, and doctoral students and 13,500 faculty and staff. The University is a member of the prestigious Association of American Universities and co-manager of the nearby Brookhaven National Laboratory, a multidisciplinary research laboratory supporting world-class scientific programs utilizing state-of-the-art facilities. Stony Brook University is also located close to the Cold Spring Harbor Laboratory with which it interacts through graduate program training and faculty collaborations. To apply, use Academic Jobs Online ( https://academicjobsonline.org/ajo/jobs/5289) to submit a State employment application, a complete curriculum vitae including publications, and a 3-page proposed research plan of current and future research, and have three letters of recommendation submitted through the AJO site. The cover letter should indicate whether the applicant wishes to be considered for appointment at the Assistant, Associate, or Full Professor level. Applicants at the Associate or Full Professor level should add a summary of past and current research funding and administrative and teaching experiences. Electronic submission through AJO is required. Questions should be addressed to Ms. Lynda Perdomo-Ayala, Department Administrator ( lynda.perdomo-ay...@stonybrook.edu). 631-444-3050 For a full position description, visit www.stonybrook.edu/jobs (Ref. F-9387/14/12.) Stony Brook University is an Affirmative Action, Equal Opportunity Educator and Employer.
[ccp4bb] Post-doc at MacCHESS in BioSAXS
The Macromolecular Diffraction Facility of the Cornell High-Energy Synchrotron Source (MacCHESS) has an opening for a Postdoctoral Associate. Applicants should have a Ph.D. degree in a relevant field (physics, engineering, structural biology etc.). Preference will be given to those with experience in x-ray solution scattering on biological systems (SAXS and WAXS). Activities will focus on developing cryogenic BioSAXS technology and implementing time-resolved BioSAXS. Projects may also involve developing novel microfluidic lab-on-a-chip methods, applying state-of-the art algorithms to data (especially as relating to mixtures of oligomers and time-resolved data) and automating data processing at the beamline. Size exclusion chromatography (SEC), multiangle and dynamic light scattering (MALS/DLS) experience is desirable, as is engineering experience developing hardware and software (incluing nanofabrication). Software development will be done primarily in Python. While MacCHESS postdocs are not required to do general beamline user support, they will be expected to help with the annual BioSAXS Essentials training course and to work closely with beamline users with whom they are collaborating. Good clear communication skills are a must, including fluency in the English language. Appointments are for one year at a time and are renewable for additional years, contingent upon availability of funds and employee performance. Located on an Ivy League university campus in picturesque upstate New York, the Cornell High-Energy Synchrotron Source (CHESS) serves a world-wide user base of structural biologists, chemists, physicists, and engineers. MacCHESS is an NIH-supported National Resource providing support for structural biology at CHESS. MacCHESS is a heavily team-oriented environment. Applications should be submitted at http://academicjobsonline.org/ (posting #5329) and should include a cover letter, a CV, a list of publications, and a detailed summary of research experience and interests. Please arrange to have at least three letters of recommendation sent, as per instructions on the academicjobsonline website. The starting date is negotiable. For more information about the position, contact Dr. Marian Szebenyi at dm...@cornell.edu. Diversity and Inclusion are a part of Cornell University’s heritage. We’re a recognized employer and educator valuing AA/EEO, Protected Veterans, and Individuals with Disabilities.
Re: [ccp4bb] ligand bonds (AlF3) breaking up after refinement in refmac
On 28/01/15 21:05, ansuman biswas wrote: Dear All, I checked the Mg2+ B factor, and it was around 22. So, were the values for F atoms. For AlF3, it was more than 50 for Al and more than 40 for F atoms. I will take care about the occupancy. I hope that will fix the small negative density. When I inserted MgF in COOT using the code MGF (get monomer), it did appear but looked fragmented. It remained fragmented after refinement as well (as shown in the previously attached fig). But, there was no warning about bond breaking in the Refmac log file. Even the density of MgF3- looked better (2Fo-Fc). If I see the structure in Chimera or CCP4MG, it does not look fragmented. So, is it a problem of display in COOT? Yes. Is the exploded MgF3 form, not actually a broken form, since the refinement log file does not show any such indication? Yes. You have stumbled across an obscure idiosyncrasy of Coot's bonding algorithm (it doesn't see bonds in residues where all the bonds are longer than 1.71A). You might call this a bug. (Incidentally the dictionary values for the bond length is 1.985A.) Paul.
