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Updated: Feb 11, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
The putative siderophore-interacting protein from Vibrio anguillarum: protein production, analysis, crystallization
Yu Han1, Kun Zang1, Changshui Liu1
1Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, Qingdao 266071, People's Republic of China.
Abstract:
Siderophore-interacting proteins (SIPs) play an important role in iron acquisition in many bacteria. SIPs release iron from the internalized ferric siderophore complex by reducing ferric iron to ferrous iron, but how the iron is reduced is not well understood. Here, a sip gene was identified in the genome of Vibrio anguillarum 775. To further understand the catalytic mechanism of the protein, the SIP was overexpressed in Escherichia coli Rosetta (DE3) cells, purified and crystallized for X-ray diffraction analysis. The crystal diffracted to 1.113 Å resolution and belonged to space group P21, with unit-cell parameters a = 64.63, b = 58.47, c = 70.65 Å, β = 114.19°.
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