Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of DsrEFH from Allochromatium vinosum
Author(s) -
Dahl Christiane,
Schulte Andrea,
Shin Dong Hae
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107041188
Subject(s) - monoclinic crystal system , crystallography , sulfur , crystallization , cloning (programming) , gene , synchrotron , chemistry , crystal structure , crystal (programming language) , protein crystallization , intracellular , bacteria , biology , biochemistry , genetics , physics , organic chemistry , computer science , nuclear physics , programming language
In purple sulfur bacteria, the proteins encoded by dsr genes play an essential role in the oxidation of intracellular sulfur, which is an obligate intermediate during the oxidation of sulfide and thiosulfate. One such gene product, DsrEFH from Allochromatium vinosum , has been cloned, expressed, purified and crystallized. Synchrotron data were collected to 2.5 Å from a crystal of selenomethionine‐substituted DsrEFH. The crystal belongs to the primitive monoclinic space group P 2 1 , with unit‐cell parameters a = 56.6, b = 183.1, c = 107.8 Å, β = 99.6°. A full structure determination is under way in order to provide insight into the structure–function relationships of this protein.