Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea.
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), with unit-cell parameters a = 38.68, b = 46.73, c = 88.9 A.
Kohoutová
J
J
Institute of Systems Biology and Ecology, Academy of Sciences of Czech Republic, Zámek 136, 37333 Nové Hrady, Czech Republic.
Kutá Smatanová
I
I
Brynda
J
J
Lapkouski
M
M
Revuelta
J L
JL
Arellano
J B
JB
Ettrich
R
R
D003460:Crystallization; D018360:Crystallography, X-Ray; D045332:Photosystem II Protein Complex / Q000032:analysis / Q000737:chemistry*; D010940:Plant Proteins / Q000032:analysis / Q000737:chemistry*; D011994:Recombinant Proteins / Q000032:analysis / Q000737:chemistry; D018724:Spinacia oleracea / Q000737:chemistry*
D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D011994:Recombinant Proteins