Jedrzejas M J, Baker J R, Luo M
Center for Macromolecular Crystallography, University of Alabama at Birmingham 35294, USA.
Proteins. 1995 May;22(1):76-8. doi: 10.1002/prot.340220112.
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 is P1, and the unit cell dimensions are a = 43.55, b = 53.11, c = 60.10 A, alpha = 90.44, beta = 106.21, gamma = 101.51 degrees. The VM of 1.8 A3/Da is consistent with the presence of two molecules of the link protein in the asymmetric unit. The crystals diffract X-rays from a synchrotron source to 1.7 A resolution.
软骨细胞外基质连接蛋白分子量约为40 kDa，是一种结合二价阳离子的金属蛋白，仅溶于低离子强度溶液。该连接蛋白从牛气管中纯化出来，并已通过气相扩散法，以聚乙二醇3350作为沉淀剂进行结晶。晶体对称性为P1，晶胞参数为a = 43.55、b = 53.11、c = 60.10 Å，α = 90.44、β = 106.21、γ = 101.51°。1.8 ų/Da的VM值与不对称单元中存在两个连接蛋白分子一致。这些晶体在同步辐射源下可将X射线衍射至1.7 Å分辨率。
