I am looking for recent Ph.D. graduates with a strong background in protein structure. Applicants should have experience in molecular biology and protein purification. Experience in crystallography or NMR is strongly preferred, but other qualified candidates will be considered. Several projects are available, some of which involve the study of membrane-bound proteins and protein-lipid interactions. The lab is located at the Ontario Cancer Institute/University of Toronto, and provides a unique environment with many opportunities for collaborative interactions between crystallographic, NMR and molecular biology labs. Please send your CV and the names of three references to : Dr. Gil Prive Ontario Cancer Institute Department of Medical Biophysics University of Toronto 500 Sherbourne Street Toronto, Ontario Canada M4X 1K9 email : prive@oci.utoronto.ca Replies via email are preferred.
Dr. Carl Creutz Dr. Robert Kretsinger
Department of Pharmacology Department of Biology
cec3n@virginia.edu rhk5i@virginia.edu
The crystal structures of annexin I (full length, human lipocortin I
or calpactin II) and of annexin VI (full length, bovine p68) are being
refined. Small crystals of annexin IV (endonexin I) are available. The
fellow may complete the refinements of annexins I and VI while developing the
annexin IV problem. We are characterizing annexins from C. elegans and from
Arabidopsis and hope to crystallize these.
Dr. Creutz has extensive experience with annexins and has available
the facilities and protocols for their expression purification, and
modification.
Dr. Kretsinger's lab has a full range of x-ray diffraction equipment,
computers, and the associated software.
The position is available July/95 at a competitive salary.
Charlottesville is a very stimulating and pleasant community. Please send
resume to RHK and have three letters of recommendation sent to R. H.
Kretsinger, Department of Biology, University of Virginia, Charlottesville,
VA. 22903 (or rhk5i@virginia.edu).
Anticipated Post Doctoral Position Diffraction and Thermophysical Properties Group Metals and Ceramics Division Oak Ridge National Laboratory The position involves interacting with industrial, academic, and federal laboratory users as part of the High Temperature Materials Laboratory User Program, assisting in DOE-sponsored programs, and participation in cooperative industrial-government research projects. Work will focus on room- and high-temperature x-ray and neutron powder diffraction as well as residual stress determination for engineering materials. Activities include training users on hardware and software and participating in experimental design, data collection, interpretation, presentations, and publications. Further responsibilities include maintenance, modification, and upgrades of existing equipment and software. Applicants must have a recent Ph.D. in materials science, materials engineering, solid state physics, or other closely related field. A thorough understanding of x- ray and/or neutron powder diffraction techniques is required, and experience with diffraction furnaces, PSDs, and stress measurement is highly desirable. Experience with modern data analysis methods, especially the Rietveld structure analysis technique, is also desirable. The ability to work in several computer environments including Apple OS, MS-DOS, VMS, and Unix is necessary, and programming experience in high-level languages, e.g. C and FORTRAN, is desirable. Outstanding oral and written communication skills are required, with emphasis on technical publication and proposal writing abilities. The candidate must have strong interpersonal skills and enjoy extensive interactions with industry, DOE, and other laboratory and university engineers, scientists, and managers. Interested individuals should send a current resume or curriculum vitae and relevant details to Dr. Camden Hubbard, Oak Ridge National Laboratory, P.O. Box 2008, Bldg. 4515, MS6064, Oak Ridge, TN 37831-6064 or e-mail to hubbardcr@ornl.gov.
A post-doctoral position is immediately available at the Chemistry
Division, Argonne National Laboratory, to participate in the design and
development of SAXS instrument at the Basic Energy Sciences Synchrotron
Research Center (BESSRC) at Argonne's APS facility and conduct research
on the characterization of synthetic clays and other catalytic materials
by using SAXS and anomalous SAXS at synchrotron x-ray facilities.
Candidates should have received their Ph.D within the past 2.5 years.
Highly desirable is experience in x-ray scattering at synchrotron facilities,
strong interest in the design and development of x-ray scattering instrument,
adequate knowledge in x-ray optics and detectors as well as capability in
software development for instrument design and controls. Interested candidates
should send their CV to
Dr. P. Thiyagarajan,
Bldg. 200, JA105,
Argonne National Laboratory,
9700 S. Cass Avenue,
Argonne, Il 60439.
Ph: 708-252-3593
e-mail: Thiyaga@anlpns.pns.anl.gov.
A position for a protein crystallographer is available at the National
Cancer Institute, Frederick, Maryland, to work in the Structural Biochemistry
Program directed by Dr John W. Erickson. The program is addressing fundamental
problems related to the area of structure-based drug design. Systems under stud
include HIV protease and drug resistant mutants, cathepsin D, and other targets
in cancer and AIDS. The program has state-of-the-art facilities and personnel
in molecular biology, biophysics, biochemistry, protein crystallography,
synthetic organic chemistry and computational chemistry. All these groups
create an exciting and unique environment in structural biology. The
determination of high resolution structures by the protein crystallography
group is critical to the operation.
The x-ray crystallography equipment includes two Rigaku RU200 generators,
R-Axis II and MAR image plate detectors, low temperature facilities and novel
Franks optics. The Structural Biochemistry Program is a dedicated research
component of NCI's Frederick Biomedical Supercomputing Center, and as such has
access to an extensive network of Silicon Graphics workstations, and main frame
computers, including two VAX 6620, a CONVEX C220 and a CRAY YMP8/128.
A PhD degree and actual experience in protein crystallography is required
for this position, together with some experience in either molecular biology o
crystallography methods development. Competitive salaries and benefits are
offered. Please, send a CV and the name of three references to:
Dr Abelardo M. Silva,
NCI, Building 322,
POBox B, Frederick, MD 21702, USA.
FAX (301) 846 6066
e-mail : abelardo@ncifcrf.gov
Protein crystallography, Uni. of Wisconsin, WI [March 8, 1995]
A position in protein crystallography will be available on or after July 1st,
1995 to study the structure of myosin subfragment-1 and a variety of
other enzymes. Good crystals are available for these projects. The work
will involve protein purification, mutagenesis, crystal growth, data
collection, model building and refinement. Facilities include two Rigaku
RU200 x-ray generators equipped with several Siemens Area Detectors.
Excellent computing and molecular graphics facilities are available for this
work. A fully equipped biochemistry laboratory and huge cold room is
available to this project. Applicants with experience in any aspect
crystallography or protein biochemistry will be considered. Salary will be
commensurate with experience. The University of Wisconsin is an Equal
Opportunity/Affirmative Action Employer.
The University of Wisconsin at Madison is situated on 908 acres of land on
the shore of Lake Mendota within one mile of the center of the city center.
Madison is a nice place to live offering a high standard of living at a
moderate cost. It is built around four lakes with its capitol building
located at the heart of the city on an isthmus between the two largest
lakes. The city is only 77 miles from Milwaukee, 146 miles from Chicago
and 258 miles from Minneapolis. There are plenty of things to do outside
the lab including sailing, fishing and cycling in the summer and ice-skating,
ice-boating and cross country skiing in the winter.
Interested individuals should send their curriculum vitae and three letters
of recommendation to:
Dr. Ivan Rayment,
Institute for Enzyme Research,
1710 University Avenue,
Madison, WI53705, U.S.A.
E-Mail: Ivan@Enzyme.wisc.edu, Tel: 608-262-0437
Fax: 608-265-2904
Last modified: 07/07/95Problems? Send mail to toscano@sdsc.edu.