Crystallization of the met repressor from Escherichia coli

J Mol Biol. 1988 Mar 5;200(1):217-9. doi: 10.1016/0022-2836(88)90348-8.

Abstract

The met repressor from Escherichia coli has been crystallized in space group P21, with unit cell dimensions a = 35.6 A, b = 62.6 A, c = 44.5 A, beta = 102.4 degrees and one aporepressor dimer per asymmetric unit. Preliminary X-ray diffraction photographs show measurable intensities to beyond 1.5 A resolution, and the crystal form is ideally suited to high-resolution crystallographic analysis (1 A = 0.1 nm).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Crystallization
  • Escherichia coli / genetics*
  • Methionine / genetics*
  • Repressor Proteins*
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • Repressor Proteins
  • Transcription Factors
  • Methionine