Dieter K. Schneider
Brookhaven National Laboratory
Bldg. 463 - P.O. Box 5000
Upton, NY 11973-5000
Dieter Schneider is a co-principal investigator in the
Macromolecular Crystallography Research Resource (PXRR) which provides
facilities and support at the National Synchrotron Light Source for the benefit
of outside and in-house investigators. The PXRR is supported by the
NIH's National Center for Research Resources and the DOE Office of Biological
and Environmental Research in its mission to create optimal facilities and
environments for macromolecular structure determination by synchrotron X-ray
diffraction. With a staff of about 25, the PXRR innovates new access
modes such as FedEx crystallography, builds new facilities, currently on the
X29 undulator, advances automation, develops remote participation software,
collaborates with outside groups, teaches novice users, and supports visting
investigators with 7day, 20 hours staff coverage.
Applications of neutron small-angle scattering for the structure
determination of macromolecular complexes are the focus of this program.
Development of scattering techniques, computational methods, and neutron
instrumentation is pursued to maintain a vigorous outside user program on the
H9B SANS Beamline at the High Flux Beam Reactor.
While the HFBR is shutdown, development of a neutron fiber diffraction
camera is continued. A dual purpose instrument for the measurement of
diffuse scattering and fibre diffraction was built jointly with the BNL
Physics Department and is being tested at the National Institute of Standards
and Technology. Neutron image plate detectors are used to record diffraction
at a high resolution. The new capabilities will be applied by structural
biologists who are deriving the organization of multicomponent macromolecular
fibrous complexes, probing the conformational changes in contractile proteins,
and determining intermolecular forces.
Additionaly, I am the beamline scientist at the
NSLS beam line X26C,
which is operated by a four-membered PRT including the BNL Biology Department,
Cold Spring Harbor Laboratory, the State University of New York at Stony
Brook, and the Georgia Research Alliance.
Neutron fibre diffraction pattern of a crystalline TMV specimen in a
of 0.7 mm diameter recorded for 10 minutes at H9B.
Soares A.S., Schneider D.K., Skinner J.M., Cowan M., Buono R., Robinson H.H., Heroux A.,
Carlucci-Dayton M., Saxena A., and Sweet R.M.
Remote access to the PXRR macromolecular crystallography facilities at the NSLS.
Synchrotron Radiation News, 21(5):17-23 (September, 2008).
Skinner J.M., Cowan M., Buono R., Nolan W., Bosshard H., Robinson H.H., Heroux A., Soares A.S., Schneider D.K. and Sweet R.M.
Integrated software for macromolecular crystallography synchrotron beamlines II: revision, robots and a database.
Acta Cryst., D62(11):1340-1347 (2006).
Shi W., Robinson H., Sullivan M., Abel D., Toomey J., Berman L.E., Lynch D., Rosenbaum G., Rakowsky G., Rock L., Nolan B.,
Shea-McCarthy G., Schneider D., Johnson E., Sweet R.M. and Chance M.R.
Beamline X29: a novel undulator source for X-ray crystallography.
J Synch Rad., 13:365-372 (2006).
Robinson H.H., Shi W., Sullivan M., Nolan W., Schneider D.K., Berman L., Lynch D., Rock L., Rosenbaum G., Johnson E., Chance M.R. and Sweet R.M.
An undulator beamline for protein crystallography at the NSLS: Commissioning and operation of X29.
Synch Rad News, 18(5):27-31 (2005).
Soares A.S., Caspar D.L.D., Weckert E., Héroux A., Hölzer K., Schroer K., Zellner J., Schneider D., Nolan W. and Sweet R.M.
Three beam interference is a sensitive measure of the efficacy of macromolecular refinement techniques.
Acta Cryst, D59(10):1716-1724 (2003).
Schneider D.K., Chen S.H., Capel M.S., Hsiao B., Kostorz G., Pedersen J.S., Timmins P. and Wignall G.D.
Issue Preface: XIth International Conference on Small-Angle Scattering (BNL, May 17-20, 1999).
J Appl Cryst, 33:(3)(2000).
Stone D.B., Timmins P.A., Schneider D.K., Krylova I., Ramos C.H.I., Reinach F.C. and Mendelson R.A.
The Effect of Regulatory Ca++ on the in situ Structures of Troponin C and Troponin I: A Neutron Scattering Study.
J Mol Biol., 281:689-704 (1998).
Imai M., Kato T. and Schneider D.
Fluctuations and growth of a cubic network observed in a nonionic surfactant system.
J Chem Phys, 106:9362-9371 (1997).
Mendelson R.A., Schneider D.K. and Stone D.B.
Conformations of Myosin Subfragment 1 ATPase Intermediates from Neutron and X-ray Scattering.
J Mol Biol., 256:1-7 (1996).
Wu C., Quesada M.A., Schneider D.K., Farinato R., Studier F.W. and Chu B.
Polyacrylamide solutions for DNA sequencing by capillary electrophoresis: mesh sizes, separation and dispersion.
Electrophoresis, 17:1103-1109 (1996).
Flanagan J.M., Wall J.S., Capel M.S., Schneider D.K. and Shanklin J.
Scanning transmission electron microscopy and small-angle scattering provide evidence that native
Escherichia coli ClpP is a tetradecamer with an axial pore.
Biochemistry, 34:10910-10917 (1995).
Graziano V., Gerchman S.E., Schneider D.K. and Ramakrishnan V.
Histone H1 is located in the interior of the chromatin 30-nm filament.
Nature, 368:351-354 (1994).
Bivin D.B., Stone D.B., Schneider D.K. and Mendelson R.A.
Cross-helix separation of tropomyosin molecules in acto-tropomyosin as determined by neutron scattering.
Biophys J., 59:880-888 (1991).
Last Modified: March 26, 2010
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