Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):357-8. doi: 10.1107/S0907444903027458. Epub 2004 Jan 23.

Abstract

Selenium-incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit-cell parameters a = 37.58, b = 40.95, c = 48.14 A, alpha = 76.93, beta = 74.04, gamma = 64.05 degrees. Five data sets were collected from a single crystal to 1.6 A using synchrotron radiation for MAD phasing. Self-rotation functions and the Matthews coefficient are consistent with two molecules in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography
  • Crystallography, X-Ray
  • Databases as Topic
  • Escherichia coli / metabolism
  • Polymerase Chain Reaction
  • Protein C / metabolism*
  • Selenium / chemistry
  • Synchrotrons
  • Temperature
  • Thermus thermophilus / metabolism*

Substances

  • Protein C
  • Selenium