Expression, purification, crystallization and preliminary X-ray diffraction analysis of the human calcium-binding protein MRP14 (S100A9)

Citation
H. Itou et al., Expression, purification, crystallization and preliminary X-ray diffraction analysis of the human calcium-binding protein MRP14 (S100A9), ACT CRYST D, 57, 2001, pp. 1174-1176
Citations number
31
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
0907-4449 → ACNP
Volume
57
Year of publication
2001
Part
8
Pages
1174 - 1176
Database
ISI
SICI code
0907-4449(200108)57:<1174:EPCAPX>2.0.ZU;2-D
Abstract
MRP14 is a protein that is specifically expressed in myeloid and epithelial cells during the stages of acute or chronic inflammatory states such as rh eumatoid arthritis or sarcoidosis. MRP14 has EF-hand motifs as Ca2+-binding sites and belongs to the S100 family of proteins. This paper deals with th e sample preparation (cloning, overexpression and purification), crystalliz ation and preliminary crystallographic analysis of recombinant human MRP14. Crystals of MRP14 were obtained by the hanging-drop vapour-diffusion metho d. MRP14 crystals belong to space group P2(1), with unit-cell parameters a = 57.59, b = 178.44, c = 61.23 Angstrom, beta = 113.17 degrees, and diffrac t to 2.1 Angstrom resolution.