Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana

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.

Figure 1

Crystals of recombinant VSP1 grown by the sitting-drop method. The crystals grew to dimensions of ∼0.02 × 0.1 × 0.15 mm.