title: Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase.
abstract: Nonglycosylated alpha-amylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2-methyl-2,4-pentanediol as the precipitant in the presence of CaCl2 at pH 9.0. The crystals are orthorhombic, space group P2(1)2(1)2(1) with unit cell dimensions of a = 53.3, b = 75.8, and c = 138.1 A. The asymmetric unit contains one amylase molecule. The solvent content is 54%. The crystals are stable to X-rays and diffract up to 2.8 A and appear to be suitable for X-ray diffraction studies.
authors.affiliation: Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214.
authors.forename: N
authors.initials: N
authors.lastname: Ramasubbu
authors.forename: K K
authors.initials: KK
authors.lastname: Bhandary
authors.forename: F A
authors.initials: FA
authors.lastname: Scannapieco
authors.forename: M J
authors.initials: MJ
authors.lastname: Levine
mesh_terms: D003460:Crystallization; D003461:Crystallography; D006801:Humans; D010306:Parotid Gland / Q000201:enzymology; D012463:Saliva / Q000737:chemistry; D000516:alpha-Amylases / Q000737:chemistry*
chemical_list: D000516:alpha-Amylases