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Crystallography related career opportunities, post docs and related positions in the crystallography community.
If you wish to place your job opportunity on the Hampton Research website, submit the details to
tech@hrmail.com.
Description:
PhD position in crystallization and structure solution of natural and appropriate variants of the sponge protein silicatein and nanobiotechnology applications
TOPIC: Research in the field of biomineralization and applications in nanobiotechnology. Biomineralization is the formation of minerals by living cells and organisms. To understand the processes involved in biomineralization (at the cutting edge between inorganic and organic world)and for nanobiotechnology applications, the structure determination of natural and appropriate variants of silicatein from marine demosponge Suberites domuncula is required. The prospective student will carry out European funded research (Marie Curie ITN network BIOMINTEC) in two of the partner institutions, NCSR Demokritos in Greece and Johannes Gutenberg-Universitaet, Mainz in Germany and will operate within a network of institutions highly specialized in biomineralisation. The project includes participation in workshops and summer schools. Motivation to travel and adapt to a different country and to integrate efficiently in a new working team is fundamental.
TYPE OF APPOINTMENT-DURATION-STARTING DATE: Full–time contracts in the two institutions (overall period 36 months), starting April 2010 at NCSR Demokritos.
PROFILE-ELIGIBILITY
Applicants should have a BS or MSc degree in chemistry, biological sciences or related sciences and £4 years research experience at the time of hiring. They can be nationals of European Union or Associated Countries, other than the country of the host organisations (Greece & Germany). Candidates from countries outside EU are also eligible. Greek or German citizens who have resided in Greece or Germany for less than 12 months in the 3 years prior to the hiring dates are also eligible.
BENEFITS
The successful candidate as a Marie Curie fellow will enjoy high salary (according to the Marie Curie guidelines with social security benefits) and additionally a mobility allowance covering family obligations, travel allowance and career exploratory allowance.
HOW TO APPLY
Applicants should forward electronically (a) their detailed CV, (b) copies of published articles, (c) names, e-mails/phone numbers of two referees to:
Dr. I. M. Mavridis
Institute of Physical Chemistry
National Center for Scientific Research “Demokritos”
Aghia Paraskevi 1520, Athens –Greece
[Post Date: March 10, 2010]
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Description:
The laboratories of Drs. L. Wayne Schultz and Tim Umland are seeking a highly motivated individual to participate in a joint interdisciplinary research project investigating Influenza A and SARS-CoV virus-host protein-protein interactions and structures. A position at the Post-Doctoral level is available, to be fill as soon as possible. Competitive applicants should have demonstrated scientific productivity and innovation at the graduate level, and possess a Ph.D., M.D., or similar degree. The successful applicant will have previous experience in all aspects of macromolecular crystallography, as well as molecular biology, protein expression and purification. They will interact with our groups to determine the crystal structures of virus-host protein complexes important in dictating host tropism. Salary and benefits are competitive, and funding is available for up to 2 years.
The Hauptman-Woodward Medical Research Institute (HWI) is a private, not-for-profit organization studying the structures and functions of macromolecules of biomedical interest. HWI houses the Department of Structural Biology of the State University of New York at Buffalo's School of Medicine and Biomedical Sciences. HWI is housed in a new building located on the Buffalo-Niagara Medical Campus, a consortium of research, clinical, and educational institutions founded to cultivate a world-class medical campus in state-of-the art facilities in downtown Buffalo, NY, USA.
To apply for a post-doctoral position, please send your CV and the names of three references to Drs. Schultz (schultz@hwi.buffalo.edu) and Umland (umland@hwi.buffalo.edu). Please visit the web site for the Laboratory for the Study of Infectious Diseases (LSID) for additional information: http://labs.hwi.buffalo.edu/lsid
The Hauptman-Woodward Institute is an Equal Opportunity Employer.
[Post Date: March 08, 2010]
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Description:
*Ben-Gurion University of the Negev (BGU) and the National Institute for Biotechnology in the Negev (NIBN) are looking for X-ray crystallographer
for their macromolecular X-ray crystallography unit.*
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*Job description*
The Head of our service macromolecular X-ray crystallography facility, is required to be responsible for "state-of-the-art“ crystallization, data collection and structure determination of proteins and
protein-ligand complexes. The successful candidate will have to train personnel in the use of X-ray crystallographic equipment, software, and robotics and provide scientific and technical guidance as needed, as well as maintain the equipment in the facility. The facility manager will also be responsible for coordinating schedules and allocation of general users time and maintain usage logs, with the guidance of the
scientific Director (Raz Zarivach, Ph.D.). The facility will also provide external services that include protein crystallization, structural determination, interpretation, assessment and documentation,
including in-depth characterization of proteins, under the supervision of the scientific director. The manager's responsibilities will include providing support for a range of projects and involve X-ray crystallographic data collection both in-house and at synchrotrons. The
facility will work closely with BGU structural biology teams.
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*Your qualifications*
To apply, you must have/ be: Ph.D. in protein x-ray crystallography; at least two years of post doctoral experience in protein structure determination; highly experienced in protein crystallization, protein and crystal handling, data collection using synchrotron and in-house equipment, and structure refinement. Prior X-ray facilities management or equipment maintenance experience is an advantage. Multitasking, management of multiple projects, and work on a timeline; excellent oral
and written communication skills are a prerequisite.
*The Facility*
The X-ray Crystallography Laboratory is equipped with a RU-H3RHB (Rigaku, Japan) rotating-anode generator, Osmic focusing mirror (Osmic, USA), MAR image plate detector (X-Ray Research, Germany), crystallization room, cold room and cooled incubators for crystal growth at different temperatures, and computer room equipped with fast computers and advanced graphics workstations. The center includes full crystallization robotics (Formulatrix system) which composed from a liquid handling robotics (Drop Setter and Formulator) and imaging and incubation robot (Rock imager 250).
*Your application*
Applicants should send their CV and the names of three references to Raz Zarivach (zarivach@bgu.ac.il).
[Post Date: March 08, 2010]
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Description:
Research Investigator in the Structural Biology Platform of the Center for Proteomic Chemistry
The work of the Center for Proteomic Chemistry lies at the intersection of the chemical and biological universe – the common theme of our activities is the systematic study of interactions of small chemical molecules with large biological macromolecules, generally proteins.
As a member of a multidisciplinary team consisting of biologists, structural scientists and chemists, your prime responsibility is to purify proteins and perform biophysical and structural studies. You will also be involved in evaluating potential new structural biology projects, coordinating the efforts of small teams towards providing structural and biophysical data to impact drug discovery projects, and representing the Structural Biology Platform in multidisciplinary project teams.
We are looking for a highly talented and motivated scientist with a PhD in biochemistry or related disciplines plus 1-3 years of postdoctoral experience in an academic or industrial setting. The ideal candidate will have extensive experience in the area of protein purification. He/she will have a sound knowledge of biochemistry, analytics, crystallography and a strong interest in the biology of human diseases. Experience in the handling membrane proteins or the use of biophysical methods to characterise protein – ligand interactions (including NMR or SPR) would be advantageous. The candidate should be strongly committed and display a high level of creativity and passion for project work. He/she will be a member of a multi-disciplinary, multi-national team of drug discovery professionals. Excellent oral and written communication skills are required.
To find out more, please visit our website www.careers.novartis.com and select Job ID 63010 BR to apply online Novartis is an equal opportunity employer
[Post Date: February 26, 2010]
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Description:
Genzyme Corporation, ranked as one of the foremost biotechnology companies in the world, is committed to providing an exceptional environment in which individuals can excel, and achieve their professional and personal goals. Genzyme Corporation has been selected by FORTUNE magazine as one of the "100 Best Companies to Work For in 2006 in the United States”. By applying for a position with Genzyme, you are taking the first step toward becoming a part of our dynamic and talented team, and hopefully sharing in our continued success.
We have a postdoctoral position open in the Fragment-Based Drug Discovery (FBDD) group in Drug and Biomaterial R&D at Genzyme Corporation in Waltham, MA. We are seeking a highly motivated recent PhD graduate in protein X-ray crystallography for a two-year position with a possible one-year extension. This position offers opportunities to work on structural biology of protein targets of therapeutic interest for FBDD approach, which involves activities from construct design to structural determination of target protein in complex with substrates or inhibitors. The successful candidate will have access to our cutting edge FBDD technology, including state of the art crystallization equipment and X-ray diffraction system.
Basic Qualifications:
PhD in structural biology or related disciplines (biochemistry, biophysics) with track record of solving X-ray crystal structures of proteins and protein complexes. Experience with construct design, protein purification, protein crystallization, data collection, structure determination and interpretation are essential.
Preferred Qualifications:
Strong background in biochemistry with in-depth understanding of ligand-protein interactions and familiarity with techniques such as ITC, surface plasmon resonance etc. to characterize proteins in support of structural biology is highly desired.
Please submit your application on line@www.genzyme.com
[Post Date: February 24, 2010]
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Description:
Applications are invited for a postdoctoral position in Dr. Fang Li's lab at the Department of Pharmacology, University of Minnesota Twin Cities. Research involves biochemical and structural studies on proteins that guide invasion and replication of important viral pathogens.
Strong background in molecular biology and protein biochemistry is required. Experience in insect cell culture and protein crystallography is preferred. Candidates must have completed PhD at the time of the appointment. Salary commensurates with experience. The position starts immediately. For more information about Dr. Li's lab, visit http://www.msi.umn.edu/~lifang/
Interested applicants should send (1) a resume, (2) a one-page summary of previous research experience, and (3) arrange three letters of recommendation to Dr. Fang Li via emai: lifang@umn.edu
[Post Date: February 22, 2010]
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Description:
The Paul Scherrer Institute is with 1300 employees the largest research centre for natural and engineering sciences in Switzerland and a worldwide leading user laboratory. Its research activities are concentrated on the three main topics of solid-state physics, energy and environmental research as well as human health.
The Swiss Light Source (SLS) is one of the most advanced synchrotron radiation sources worldwide. The SLS operates two state-of-the-art undulator beam lines for protein crystallography, and a third, highly automated beam line located at a superbend magnet (X06DA). At beam line X06DA a crystallisation facility which is integrated with the beam line in order to allow for in situ X-ray diffraction screening is being implemented. The Macromolecular Crystallography Group (MX-Group) is involved in several aspects of protein crystallography including the design and construction of new beam line components as well as various structural biology projects, especially in collaboration with the Biomolecular Research Group at our institute under the guidance of Prof. Dr Gebhard Schertler.
We are looking for a
Postdoctoral Fellow in protein crystallisation
Your tasks
You will coordinate and ultimately lead our efforts to further establish the high-throughput crystallisation facility and its integration with beam line X06DA at the Swiss Light Source. In collaboration with the scientists and engineers of the SLS MX-Group as well as the PSI structural biology unit you will additionally further develop the in situ X-ray diffraction screening capabilities of the facility and coordinate its integration with the sample data base. In addition, there are excellent opportunities to pursue your own research projects in protein crystallography.
Your profile
You hold a PhD degree in biology or (bio-)chemistry, and have experience in either protein crystallography or high-throughput methods in crystallisation. Experience in synchrotron related research or with data bases is a plus. If you are self-motivated and a good team player this position will offer great opportunities to start your research career in an exciting and highly multidisciplinary environment.
For further information please contact: Dr Rouven Bingel-Erlenmeyer, phone +41 56 310 58 23, rouven.bingel-erlenmeyer@psi.ch or Dr Clemens Schulze-Briese, phone +41 56 310 45 33, clemens.schulze@psi.ch
Please submit your application to: Paul Scherrer Institut, Human Resources, Ref. code 6112, Elke Baumann, 5232 Villigen PSI, Switzerland or to: elke.baumann@psi.ch
[Post Date: February 22, 2010]
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Description:
Applications are invited for a Wellcome Trust funded position to investigate the structure, assembly and functioning of nuclear receptor co-regulator complexes. The appointee will join the research group of Professor John Schwabe working in the newly-appointed Henry Wellcome Laboratories of Structural Biology.
The successful applicants will hold a PhD in a relevant subject, or be in the process of submitting a PhD in a relevant subject, and will have experience in molecular biological and biochemical techniques.
Informal enquiries are welcome and should be made directly to Professor John Schwabe john.schwabe@le.ac.uk
Please see the links below if you are interested in finding out more.
http://www2.le.ac.uk/offices/personnel/job-vacancies/?newms=jj&id=59761
http://www2.le.ac.uk/departments/biochemistry/staff/schwabe/john-schwabes-research-pages
[Post Date: February 17, 2010]
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Description:
Structure-function studies on protein-RNA complexes
A postdoctoral position is available immediately in the group of Dr. Graeme L. Conn at Emory University School of Medicine in Atlanta GA, USA. Our lab uses X-ray crystallography and complementary biochemical and biophysical methods to address macromolecular structure, interactions and function. The post is available on an on-going project investigating host cell protein-viral non-coding RNA complexes.
Our laboratory is located in recently renovated space in the Department of Biochemistry where we are one of four groups with diverse research interests that form a critical mass in the areas of X-ray crystallography and structural biology. We have access to state-of-the-art crystallization and in-house X-ray data collection facilities as well as dedicated synchrotron beamtime at the Advanced Photon Source (APS) SER-CAT beamline.
Interested applicants must have a Ph.D. in biochemistry, molecular biology or structural biology and experience working with RNA would be an advantage. X-ray crystallographic experience is strongly preferred but not essential. The ideal candidate will be highly motivated, possess excellent communication skills and the ability to work in a collaborative and team-oriented environment.
To apply, please e-mail a cover letter including a brief statement of experience and scientific interests, a CV with a list of publications and contact information for three references to: gconn@emory.edu. Informal enquiries are also welcome at the same email address. Review of applications will begin immediately and continue until the post is filled.
Further details about the Department of Biochemistry and our research can be found here:
http://www.biochem.emory.edu/
http://www.biochem.emory.edu/cgi-bin/people/detail_faculty?id=gconn
[Post Date: February 16, 2010]
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Title:
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Research Scientist Duke University
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Description:
RESEARCH SCIENTIST, CRYSTALLOGRAPHY FACILITY
The Human Vaccine Institute at Duke University is currently seeking a Research Scientist to join the Macromolecular X-ray Crystallography and Small Molecule X-Ray Crystallography labs. The Research Scientist will assist facility users in a variety of crystallography-specific and related tasks including training users in safe and proper use of equipment / software and advising users on experimental designs and strategies (such as providing guidance on selecting screens for initial crystallization trials; repeating, optimizing and translating hit conditions; data collection strategies; data processing assistance; phasing, rebuilding and refining structures) as well as troubleshooting problems and performing regularly scheduled maintenance on equipment.
Qualified candidates should have a Ph.D. in a scientific discipline or in the health or physical sciences with a minimum of two years’ specific experience with X-ray crystallography. Experience with crystallography robotics, crystallography software, small molecule crystallography, protein purification, and hardware maintenance is desired.
Interested candidates should submit a resume and three references to:
Nathan Nicely, Ph.D.
DHVI.Careers@notes.duke.edu
Please note “XRC” in the subject line.
Duke University Medical Center is located in the energetic and progressive Research Triangle area of North Carolina and has been named a Best Employer.
Duke University and Health Systems is an Equal Opportunity Employer
[Post Date: January 21, 2010]
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TECHNICAL SUPPORT
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Tel: 949-425-1321
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Fax: 949-425-1611
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Email: tech@hrmail.com
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LOCATION
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Hampton Research
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34 Journey
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Aliso Viejo, CA 92656-3317
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Toll Free: 800-452-3899
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Tel: 949-425-1321
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Fax: 949-425-1611
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BUSINESS HOURS
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7:00 am to 5:00pm
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Monday - Friday
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(Pacific Standard Time)
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