Cloning, purification, crystallization and preliminary X-ray analysis of the Burkholderia pseudomallei L1 ribosomal protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):347-50. doi: 10.1107/S1744309112004800. Epub 2012 Feb 22.

Abstract

The gene encoding the L1 ribosomal protein from Burkholderia pseudomallei strain D286 has been cloned into the pETBLUE-1 vector system, overexpressed in Escherichia coli and purified. Crystals of the native protein were grown by the hanging-drop vapour-diffusion technique using PEG 3350 as a precipitant and diffracted to beyond 1.65 Å resolution. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 53.6, b = 127.1, c = 31.8 Å and with a single molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Burkholderia pseudomallei / chemistry*
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / isolation & purification

Substances

  • Ribosomal Proteins
  • ribosomal protein L1