Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea

Kohoutová, Jaroslava; Kutá-Smatanová, Ivana; Brynda, Jiří; Lapkouski, Mikalai; Revuelta, J. L.; Arellano, J.B.; Ettrich, Rüdiger

doi:https://dx.doi.org/10.1107/S1744309108040578

Number of the records: 1

Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea

1.

SYSNO ASEP	0343418
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea
Author(s)	Kohoutová, Jaroslava (UEK-B) Kutá-Smatanová, Ivana (UEK-B)_RID Brynda, Jiří (UOCHB-X)_{RID, ORCID} Lapkouski, Mikalai (UEK-B) Revuelta, J. L. (ES) Arellano, J.B. (ES) Ettrich, Rüdiger (UEK-B)_{RID, ORCID, SAI}
Number of authors	7
Source Title	Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091 F65, č. 2 (2009), s. 111-115
Number of pages	5 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	photosystem protein ; crystallization ; X-ray analysis
Subject RIV	CC - Organic Chemistry
R&D Projects	LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z40550506 - UOCHB-X (2005-2011)
	AV0Z60870520 - UEK-B (2005-2011)
UT WOS	000263071400011
DOI	10.1107/S1744309108040578
Annotation	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).
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418
Year of Publishing	2011

Number of the records: 1