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Crystallization, preliminary crystallographic analysis and phasing of the thiosulfate-binding protein SoxY from Chlorobium limicola f. thiosulfatophilum

Journal Article · · Acta Crystallographica. Section F
;  [1]; ;  [2]
  1. Department of Biochemistry, Physiology and Microbiology, Laboratory for Protein Biochemistry and Protein Engineering, K. L. Ledeganckstraat 35, Ghent University, 9000 Ghent (Belgium)
  2. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22063 Hamburg (Germany)
SoxY from C. limicola f. thiosulfatophilum is involved in thiosulfate metabolism. Crystallization, preliminary crystallographic analysis and phasing of this protein are presented. The 22 kDa SoxYZ protein complex from the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum is a central player in the sulfur-oxidizing (Sox) enzyme system of the organism by activating thiosulfate for oxidation by SoxXA and SoxB. It has been proposed that SoxYZ exists as a heterodimer or heterotetramer, but the properties and role of the individual components of the complex thus far remain unknown. Here, the heterologous expression, purification, and the crystallization of stable tetrameric SoxY are reported. Crystals of SoxY diffract to 2.15 Å resolution and belong to space group C222{sub 1}, with unit-cell parameters a = 41.22, b = 120.11, c = 95.30 Å. MIRAS data from Pt{sup 2+}- and Hg{sup 2+}-derivatized SoxY crystals resulted in an interpretable electron-density map at 3 Å resolution after density modification.
OSTI ID:
22356399
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 11 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English