Open AccessCrystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana
Author(s) -
Shi ZhuBing,
Ge HongHua,
Zhao Ping,
Zhang Min
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109053688
Subject(s) - arabidopsis thaliana , crystallization , recombinant dna , crystallography , molecular replacement , resolution (logic) , arabidopsis , protein crystallization , crystal (programming language) , escherichia coli , x ray crystallography , diffraction , chemistry , materials science , crystal structure , biochemistry , physics , gene , optics , organic chemistry , mutant , artificial intelligence , computer science , programming language
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 Å resolution and a complete X‐ray data set was collected at 100 K using Cu K α radiation from a rotating‐anode X‐ray source. The crystals belonged to space group C 2. 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.