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Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana.

Authors :
Shi, Zhu-Bing
Ge, Hong-Hua
Zhao, Ping
Zhang, Min
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Feb2010, Vol. 66 Issue 2, p201-203. 3p.
Publication Year :
2010

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 Å resolution and a complete X-ray data set was collected at 100 K using Cu Kα 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
66
Issue :
2
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
110812402
Full Text :
https://doi.org/10.1107/S1744309109053688