Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Aug 1;61(Pt 8):782-4. doi: 10.1107/S1744309105022839. Epub 2005 Jul 30.

Abstract

Diaminopimelate decarboxylase from Mycobacterium tuberculosis (LysA, DAPDC, Rv1293) has been cloned and heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized. Preliminary diffraction data analysis suggests the presence of a homotetramer in the asymmetric unit.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / isolation & purification*
  • Cloning, Molecular
  • Crystallization
  • Gene Expression*
  • Mycobacterium tuberculosis / chemistry*
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Carboxy-Lyases
  • LysA protein, Bacteria