Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana
- PMID: 20124723
- PMCID: PMC2815693
- DOI: 10.1107/S1744309109053688
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.
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References
-
- Allen, K. N. & Dunaway-Mariano, D. (2004). Trends Biochem. Sci.29, 495–503. - PubMed
-
- Berger, S., Bell, E., Sadka, A. & Mullet, J. E. (1995). Plant Mol. Biol.27, 933–942. - PubMed
-
- Berger, S., Mitchell-Olds, T. & Stotz, H. U. (2002). Physiol. Plant.114, 85–91. - PubMed
-
- Bradford, M. M. (1976). Anal. Biochem.72, 248–254. - PubMed
-
- Burroughs, A. M., Allen, K. N., Dunaway-Mariano, D. & Aravind, L. (2006). J. Mol. Biol.361, 1003–1034. - PubMed
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