Expression, crystallization and preliminary crystallographic analysis of YciE, a stress protein from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1888-9. doi: 10.1107/S0907444904018591. Epub 2004 Sep 23.

Abstract

The stress protein Escherichia coli YciE was overexpressed and purified in three chromatographic steps. Crystals were obtained using PEG 4000 as a precipitant. The YciE protein crystals diffracted to 3.0 A resolution using a rotating-anode X-ray source. The lattice type is rhombohedral, with unit-cell parameters a = b = 64.2, c = 167.9 A, alpha = beta = 90, gamma = 120 degrees. The crystal belongs to space group R32.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray / methods*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism
  • Recombinant Proteins / chemistry
  • X-Rays

Substances

  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • Recombinant Proteins
  • YciE protein, E coli