Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase.
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.
Ramasubbu
N
N
Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214.
Bhandary
K K
KK
Scannapieco
F A
FA
Levine
M J
MJ
D003460:Crystallization; D003461:Crystallography; D006801:Humans; D010306:Parotid Gland / Q000201:enzymology; D012463:Saliva / Q000737:chemistry; D000516:alpha-Amylases / Q000737:chemistry*
D000516:alpha-Amylases