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.