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Expression, purification and preliminary crystallographic analysis of a haem‐utilizing protein, HutX, from Vibrio cholerae
Author(s) -
Su Tiantian,
Chi Kaikai,
Wang Kang,
Guo Liming,
Huang Yan
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14027666
Subject(s) - vibrio cholerae , orthorhombic crystal system , operon , cytoplasm , chemistry , crystallography , strain (injury) , vibrio , biology , biochemistry , bacteria , escherichia coli , crystal structure , genetics , gene , anatomy
Vibrio cholerae , the causative agent of cholera, has developed a variety of mechanisms to obtain the limited‐availability iron from human hosts. One important method for iron acquisition is through haem‐uptake systems. Although the transport of haem has been widely studied, the fate of haem once it enters the cytoplasm remains an open question. Here, preliminary X‐ray crystallographic analysis was performed on HutX, a member of the conserved haem‐utilization operon from V. cholerae strain N16961. The crystals of HutX were found to belong to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 50.1, b = 169.0, c = 81.8 Å. There are two protein molecules in the asymmetric unit, with a corresponding Matthews coefficient V M of 2.06 Å 3 Da −1 and a solvent content of 40.28%.