Literature DB >> 20124723

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

Zhu-Bing Shi1, Hong-Hua Ge, Ping Zhao, Min Zhang.   

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.

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Year:  2010        PMID: 20124723      PMCID: PMC2815693          DOI: 10.1107/S1744309109053688

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  16 in total

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Authors: 
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Authors:  C Ellis; J G Turner
Journal:  Plant Cell       Date:  2001-05       Impact factor: 11.277

9.  Arabidopsis thaliana Atvsp is homologous to soybean VspA and VspB, genes encoding vegetative storage protein acid phosphatases, and is regulated similarly by methyl jasmonate, wounding, sugars, light and phosphate.

Authors:  S Berger; E Bell; A Sadka; J E Mullet
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  1 in total

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  1 in total

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