Expression, purification, crystallization and preliminary diffraction studies of the mammalian DAG kinase homologue YegS from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):295-7. doi: 10.1107/S1744309106004799. Epub 2006 Feb 28.

Abstract

yegS is a gene encoding a 32 kDa cytosolic protein with unknown function but with strong sequence homology to a family of structurally uncharacterized eukaryotic non-protein kinases: diacylglycerol kinases, sphingosine kinases and ceramide kinases. Here, the overexpression, crystallization and preliminary diffraction analysis of Escherichia coli YegS are reported. The crystals belong to space group P2(1), with unit-cell parameters a = 42.4, b = 166.1, c = 48.5 A, beta = 96.97 degrees. The presence of a dimer in the asymmetric unit was estimated to give a Matthews coefficient (VM) of 2.5 A3 Da(-1) and a solvent content of 50.8%(v/v). Single-wavelength diffraction data were collected to a resolution of 1.9 A using synchrotron radiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods
  • Crystallography, X-Ray
  • Diacylglycerol Kinase / chemistry*
  • Diacylglycerol Kinase / isolation & purification
  • Escherichia coli / chemistry*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / biosynthesis
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / isolation & purification

Substances

  • Escherichia coli Proteins
  • Diacylglycerol Kinase