CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE CARTILAGE LINK PROTEIN FROM BOVINE TRACHEA

Cartilage extracellular matrix link protein, having molecular mass of approximately 40 kDa, is a metalloprotein that binds divalent cations and is only soluble in low ionic strength solutions. The link protein was purified from bovine trachea and has been crystallized by a vapor diffusion method using PEG 3350 as precipitant. The crystal symmetry i s P1, and the unit cell dimensions are a = 43.55, b = 53.11, c = 60.10 Angstrom, alpha = 90.44, beta = 106.21, gamma = 101.51 degrees. The V -M of 1.8 Angstrom(3)/Da is consistent with the presence of two molecu les of the link protein in the asymmetric unit. The crystals diffract X-rays from a synchrotron source to 1.7 Angstrom resolution. (C) 1995 Wiley-Liss, Inc.