ArticleActa crystallographica. Section F, Structural biology communications2015
Expression, purification and preliminary crystallographic analysis of a haem-utilizing protein, HutX, from Vibrio cholerae.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
- New Insight into the Mechanism of Anaerobic Heme Degradation.Biochemistry · 2019Article
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5 authors.
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Abstract
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 C2221, 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 VM of 2.06 Å(3) Da(-1) and a solvent content of 40.28%.
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