Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12

S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit‐cell dimensions a = b = 99.6 c = 64.2 Å. There are two monomers per asymmetric unit, with a solvent content of 57...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2000-02, Vol.56 (2), p.189-191
Hauptverfasser: Moroz, Olga V., Antson, Alfred A., Dodson, G. Guy, Wilson, Keith S., Skibshøj, Inge, Lukanidin, Eugene M., Bronstein, Igor B.
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Sprache:eng
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Zusammenfassung:S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit‐cell dimensions a = b = 99.6 c = 64.2 Å. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 Å resolution and complete X‐ray data have been collected to 2.5 Å on a conventional laboratory source.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999014936