title: Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii.
abstract: This report is the first crystallographic study of an amylase from an organism that is both thermophilic and halophilic. alpha-Amylase from the thermophilic halophile Halothermothrix orenii (AmyA) is a 515-residue protein. It is stable and significantly active at 338 K in starch solution containing NaCl [up to 25%(w/v)]. Purified recombinant AmyA protein crystallizes in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 55.126, b = 61.658, c = 147.625 A, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.89 A.
authors.affiliation: Laboratory of X-ray Crystallography, Institute of Molecular and Cell Biology, 30 Medical Drive, National University of Singapore, Singapore 117609, Singapore.
authors.forename: Nan
authors.initials: N
authors.lastname: Li
authors.forename: Bharat K C
authors.initials: BK
authors.lastname: Patel
authors.forename: Benjamin N
authors.initials: BN
authors.lastname: Mijts
authors.forename: Kunchithapadam
authors.initials: K
authors.lastname: Swaminathan
mesh_terms: D001426:Bacterial Proteins; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D000516:alpha-Amylases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000516:alpha-Amylases