Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 111-115Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108040578
Keywords
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Funding
- Institutional Research Concept of the Academy of Science of the Czech Republic [AVOZ60870520, AVOZ50520514, AVOZ0550506]
- Ministry of Education of the Czech Republic [LC 06010, MSM6007665808]
- Grant Agency of the Czech Republic [203/08/0114]
- Ministerio de Education y Ciencia, Spain [BFU2007-68107-C02-02/BMC, AGL2005-07245-C03-03]
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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 angstrom resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 38.68, b = 46.73, c = 88.9 angstrom.
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