Crystallization and preliminary X-ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1272-4. doi: 10.1107/S1744309113026638. Epub 2013 Oct 30.

Abstract

Adenylate kinase plays a very important role in regulating adenylate species in the cell. Methanocaldococcus jannaschii is a rich resource of unique enzymes. Here, MJ0458, an adenylate kinase from M. jannaschii, was crystallized. A set of X-ray diffraction data to 2.70 Å resolution was collected on beamline BL-17U of the Shanghai Synchrotron Radiation Facility (SSRF). The crystal belonged to space group P4(1)2(1)2 or P4(3)2(1)2. The unit-cell parameters were a = b = 76.18, c = 238.70 Å, α = β = γ = 90°.

Keywords: MJ0458; Methanocaldococcus jannaschii; adenylate kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylate Kinase / chemistry*
  • Crystallization
  • Electrophoresis, Polyacrylamide Gel
  • Methanocaldococcus / enzymology*
  • Recombinant Proteins / chemistry
  • X-Ray Diffraction

Substances

  • Recombinant Proteins
  • Adenylate Kinase