CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF CALGRANULIN-C, A S100-LIKE CALCIUM-BINDING PROTEIN FROM PIG GRANULOCYTES

Authors
NONATO MC GARRATT RC SCHLEICHER CH SANTOME JA OLIVA G
Citation
Mc. Nonato et al., CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF CALGRANULIN-C, A S100-LIKE CALCIUM-BINDING PROTEIN FROM PIG GRANULOCYTES, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 200-202
Citations number
17
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
2
Pages
200 - 202
Database
ISI
SICI code
0907-4449(1997)53:<200:CAPCSO>2.0.ZU;2-X
Abstract
Calgranulin C (CAGC) from pig granulocytes has been crystallized and X -ray diffraction data have been collected to 2.6 Angstrom resolution. The crystals belong to the trigonal system, space group P3(1)21 or P3( 2)21, cell parameters a = b = 54.35 (2), c = 141.32(5)Angstrom and pro bably contain two molecules in the asymmetric unit. CAGC is amongst th e first reported typical S100-like calcium-binding protein to be cryst allized and studied by X-ray crystallography.