title: 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.
authors.affiliation: School of Life Science, Anhui University, Hefei 230039, People's Republic of China.
authors.forename: Zhu-Bing
authors.initials: ZB
authors.lastname: Shi
authors.forename: Hong-Hua
authors.initials: HH
authors.lastname: Ge
authors.forename: Ping
authors.initials: P
authors.lastname: Zhao
authors.forename: Min
authors.initials: M
authors.lastname: Zhang
mesh_terms: D017360:Arabidopsis / Q000737:chemistry*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D029681:Arabidopsis Proteins; D011994:Recombinant Proteins; C441479:VSP1 protein, Arabidopsis; D010450:Endopeptidases