title: Crystallization and preliminary X-ray diffraction studies of the cartilage link protein from bovine trachea.
abstract: 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.
authors.affiliation: Center for Macromolecular Crystallography, University of Alabama at Birmingham 35294, USA.
authors.forename: M J
authors.initials: MJ
authors.lastname: Jedrzejas
authors.forename: J R
authors.initials: JR
authors.lastname: Baker
authors.forename: M
authors.initials: M
authors.lastname: Luo
mesh_terms: D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D016326:Extracellular Matrix Proteins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D011509:Proteoglycans / Q000737:chemistry*; D014132:Trachea / Q000737:chemistry*; D000099249:Proteoglycan Link Protein
chemical_list: D016326:Extracellular Matrix Proteins; D011506:Proteins; D011509:Proteoglycans; D000099249:Proteoglycan Link Protein