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Updated: Aug 19, 2026

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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12
O V Moroz1, A A Antson, G G Dodson
1Structural Biology Centre, Department of Chemistry, University of York, York YO1 5DD, England.
Acta Crystallographica. Section D, Biological Crystallography
|February 10, 2000
Abstract:
S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca(2+). Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 A. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 A resolution and complete X-ray data have been collected to 2.5 A on a conventional laboratory source.

