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

Authors
Moroz, OV Antson, AA Dodson, GG Wilson, KS Skibshoj, I Lukanidin, EM Bronstein, IB
Citation
Ov. Moroz et al., Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12, ACT CRYST D, 56, 2000, pp. 189-191
Citations number
27
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
2
Pages
189 - 191
Database
ISI
SICI code
0907-4449(200002)56:<189:CAPXDA>2.0.ZU;2-O
Abstract
S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals be long to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 Angstrom. There are two monomers per asymmetric unit, with a solvent conten t of 57.9%. The crystals diffract to at least 2.2 Angstrom resolution and c omplete X-ray data have been collected to 2.5 Angstrom on a conventional la boratory source.