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 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.
Moroz
O V
OV
Structural Biology Centre, Department of Chemistry, University of York, York YO1 5DD, England.
Antson
A A
AA
Dodson
G G
GG
Wilson
K S
KS
Skibshoj
I
I
Lukanidin
E M
EM
Bronstein
I B
IB
D002135:Calcium-Binding Proteins / Q000097:blood / Q000737:chemistry* / Q000502:physiology; D003460:Crystallization; D019281:Dimerization; D005544:Forecasting; D006801:Humans; D009504:Neutrophils / Q000737:chemistry; D009418:S100 Proteins; D000067616:S100A12 Protein; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D002135:Calcium-Binding Proteins; D009418:S100 Proteins; D000067616:S100A12 Protein; C090441:S100A12 protein, human