Crystallization and preliminary crystallographic analysis of the putative sugar-binding protein Msmeg_0515 (AgaE) from Mycobacterium smegmatis

Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):189-93. doi: 10.1107/S2053230X15000035. Epub 2015 Jan 28.

Abstract

Msmeg_0515, a gene from Mycobacterium smegmatis strain 155 encoding the ligand-binding domain, AgaE, of a putative ABC sugar transporter system, has been cloned into a pET-28a vector system, overexpressed in Escherichia coli and purified. The truncated protein lacking the first 27 residues, which correspond to a N-terminal signal sequence, was crystallized using the sitting-drop vapour-diffusion technique. The crystals of this protein diffracted to 1.48 Å resolution and belonged to space group P212121, with unit-cell parameters a = 64.06, b = 69.26, c = 100.74 Å, α = β = γ = 90° and with one molecule in the asymmetric unit.

Keywords: AgaE; Msmeg_0515; Mycobacterium smegmatis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Ligands
  • Molecular Sequence Data
  • Mycobacterium smegmatis / chemistry*
  • Receptors, Cell Surface / chemistry*

Substances

  • Bacterial Proteins
  • Ligands
  • Receptors, Cell Surface
  • saccharide-binding proteins