Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):758-60. doi: 10.1107/s090744490300372x. Epub 2003 Mar 25.

Abstract

MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Histocompatibility Antigens Class I / biosynthesis*
  • Histocompatibility Antigens Class I / chemistry*
  • Histocompatibility Antigens Class I / isolation & purification
  • Plasmids / genetics
  • Streptococcus pneumoniae / chemistry*
  • Streptococcus pneumoniae / genetics*
  • X-Ray Diffraction

Substances

  • Histocompatibility Antigens Class I
  • MHC class I-related chain A