Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):201-3. doi: 10.1107/S1744309109053688. Epub 2010 Jan 28.

Abstract

VSP1 is a defence protein in Arabidopsis thaliana that may also be involved in control of plant development. The recombinant protein has been overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to 1.9 A resolution and a complete X-ray data set was collected at 100 K using Cu Kalpha radiation from a rotating-anode X-ray source. The crystals belonged to space group C2. As there are no related structures that could be used as a search model for molecular replacement, work is in progress on experimental phasing using heavy-atom derivatives and selenomethionine derivatives.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / chemistry*
  • Arabidopsis Proteins / chemistry*
  • Crystallography, X-Ray
  • Endopeptidases / chemistry*
  • Recombinant Proteins / chemistry

Substances

  • Arabidopsis Proteins
  • Recombinant Proteins
  • VSP1 protein, Arabidopsis
  • Endopeptidases