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Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea
- 1.0343418 - ÚOCHB 2011 RIV GB eng J - Journal Article
Kohoutová, Jaroslava - Kutá-Smatanová, Ivana - Brynda, Jiří - Lapkouski, Mikalai - Revuelta, J. L. - Arellano, J.B. - Ettrich, Rüdiger
Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. F65, č. 2 (2009), s. 111-115. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA MŠMT(CZ) LC06010
Institutional research plan: CEZ:AV0Z40550506; CEZ:AV0Z60870520
Keywords : photosystem protein * crystallization * X-ray analysis
Subject RIV: CC - Organic Chemistry
Impact factor: 0.551, year: 2009
Preliminary X-ray diffraction analysis of the extrinsic PsbP protein of photosystem II from spinach (Spinacia oleracea) was performed using N-terminally His-tagged recombinant PsbP protein overexpressed in Escherichia coli. Recombinant PsbP protein (thrombin-digested recombinant His-tagged PsbP) stored in bis-Tris buffer pH 6.00 was crystallized using the sitting-drop vapour-diffusion technique with PEG 550 MME as a precipitant and zinc sulfate as an additive. SDS-PAGE analysis of a dissolved crystal showed that the crystals did not contain the degradation products of recombinant PsbP protein. PsbP crystals diffracted to 2.06 A resolution in space group P2(1)2(1)2(1).
Permanent Link: http://hdl.handle.net/11104/0185901
Number of the records: 1