Abstract

Utilization of a very small anomalous diffraction signal provided by sulfur atoms of the cysteine and methionine residues, intrinsically present in all proteins can be succssfully used to solve crystal structures of proteins. This approach, in part pioneered by us, is currently gaining increasoing popularity and may become a routine technique in the practice of macromolecular crystallography. The diffraction data to extremely high resolution of 0.65 angstrom were measured using synchrotron radiation, and the refined model reveals the unprecedented structgural details of the molecule of lysozyme. The observed very fine features in this structure will serve to improve the stereochemical libraries used for routine refinement of protein crystal structures at lower resolution. We participated in several collaborative structural projects on various biologically important proteins, such as the studies of the bacterial and human enzymes active in the mitochondrial mRNA degradosome.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Intramural Research (Z01)
Project #
1Z01BC010378-09
Application #
7733016
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
9
Fiscal Year
2008
Total Cost
$1,514,082
Indirect Cost

  Institution

Name
National Cancer Institute Division of Basic Sciences
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

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

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