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

Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1217-9. doi: 10.1107/s0907444902007369. Epub 2002 Jun 20.

Abstract

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 A using synchrotron radiation. The crystals belong to the primitive orthorhombic system, with unit-cell parameters a = 50.56, b = 63.45, c = 168.02 A. The asymmetric unit contains two monomers of the protein, with a corresponding V(M) of 2.25 A(3) Da(-1) and a solvent content of 44.84%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray / methods*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Molecular Chaperones / chemistry*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Synchrotrons

Substances

  • Escherichia coli Proteins
  • Molecular Chaperones
  • Recombinant Proteins
  • hchA protein, E coli