Crystallization and preliminary X-ray crystallographic analysis of a yedU gene product from Escherichia coli

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A yedU gene product with a molecular mass of 31 kDa is a hypothetical protein with no known function. The protein was purified and crystallized at 296 K. X-ray diffraction data have been collected to 2.3 Angstrom using synchrotron radiation. The crystals belong to the primitive orthorhombic system, with unit-cell parameters a = 50.56, b = 63.45, c = 168.02 Angstrom. The asymmetric unit contains two monomers of the protein, with a corresponding V-M of 2.25 Angstrom(3) Da(-1) and a solvent content of 44.84%.
Publisher
BLACKWELL MUNKSGAARD
Issue Date
2002-07
Language
English
Article Type
Article
Keywords

PROTEIN H-NS; DNA-BINDING PROTEIN; INTRACELLULAR PROTEASE; MOLECULAR ANALYSIS; CRYSTAL-STRUCTURE; NUCLEOID PROTEIN; EXPRESSION; HNS; DATABASE; CATALASE

Citation

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.58, no.7, pp.1217 - 1219

ISSN
0907-4449
URI
http://hdl.handle.net/10203/85773
Appears in Collection
BS-Journal Papers(저널논문)
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