The aim of the research within this Section is to utilize the unique properties of the X-ray radiation generated at synchrotron storage rings u in particular, at beamline X9B of the National Synchrotron Light Source, Brookhaven National Laboratory. The two most important characteristics of synchrotron radiation are the high intensity of the X-ray beam and the tunability of the wavelength; both of these properties are utilized in the research investigations within the Section. In addition to conducting research investigations, the Section personnel provides technological and scientific support for NIH researchers collecting diffraction data at beamline X9B of the National Synchrotron Light Source. The NIH Intramural Synchrotron Consortium of macromolecular crystallographers is a part of the Participating Research Team and uses 37.5% of the total available time at beamline X9B, which is equivalent to about 25 days per four-month scheduling period. Collecting diffraction data at the synchrotron beamline involves a very high level of technology u but it is a scientific process, not a technicality. Therefore, a proper selection of all the necessary parameters can be done only if based on scientific considerations. The Synchrotron Radiation Research Section supports the users of beamline X9B in all aspects of diffraction data collection.

Agency
National Institute of Health (NIH)
Institute
Division of Basic Sciences - NCI (NCI)
Type
Intramural Research (Z01)
Project #
1Z01BC010378-02
Application #
6559238
Study Section
Mammalian Cell Lines Committee (MCL)
Project Start
Project End
Budget Start
Budget End
Support Year
2
Fiscal Year
2001
Total Cost
Indirect Cost
Name
Basic Sciences
Department
Type
DUNS #
City
State
Country
United States
Zip Code
Jaskolski, Mariusz; Gilski, Miroslaw; Dauter, Zbigniew et al. (2007) Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them? Acta Crystallogr D Biol Crystallogr 63:611-20
Meijers, Rob; Adolph, Hans-Werner; Dauter, Zbigniew et al. (2007) Structural evidence for a ligand coordination switch in liver alcohol dehydrogenase. Biochemistry 46:5446-54
Jedrzejczak, Robert; Dauter, Zbigniew; Dauter, Miroslawa et al. (2006) Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails. Acta Crystallogr D Biol Crystallogr 62:157-64
Bielnicki, Jakub; Devedjiev, Yancho; Derewenda, Urszula et al. (2006) B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins 62:144-51
Sekar, K; Yogavel, M; Kanaujia, Shankar Prasad et al. (2006) Suggestive evidence for the involvement of the second calcium and surface loop in interfacial binding: monoclinic and trigonal crystal structures of a quadruple mutant of phospholipase A2. Acta Crystallogr D Biol Crystallogr 62:717-24
Liu, Yizhou; Cheney, Matthew D; Gaudet, Justin J et al. (2006) The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity. Cancer Cell 9:249-60
Dauter, Zbigniew (2006) Estimation of anomalous signal in diffraction data. Acta Crystallogr D Biol Crystallogr 62:867-76
Sekar, K; Yogavel, M; Gayathri, D et al. (2006) Atomic resolution structure of the double mutant (K53,56M) of bovine pancreatic phospholipase A2. Acta Crystallogr Sect F Struct Biol Cryst Commun 62:1-5
Dauter, Zbigniew (2006) Current state and prospects of macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 62:1-11
Serganov, Alexander; Keiper, Sonja; Malinina, Lucy et al. (2005) Structural basis for Diels-Alder ribozyme-catalyzed carbon-carbon bond formation. Nat Struct Mol Biol 12:218-24

Showing the most recent 10 out of 40 publications