title: Crystallization of a novel alpha-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii.
abstract: This is a report on the structure determination of AmyB, the second alpha-amylase from Halothermothrix orenii, by X-ray crystallography. This bacterium was isolated from saltpans where conditions consisted of both high temperatures and high NaCl content. AmyB is a 599-residue protein which is stable and significantly active at 358 K in starch solution containing up to 10%(w/v) NaCl. The purified recombinant AmyB protein crystallizes in the monoclinic space group C2, with unit-cell parameters a = 225.85, b = 77.16, c = 50.13 A, beta = 99.32 degrees, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.97 A.
authors.affiliation: Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
authors.forename: Tien-Chye
authors.initials: TC
authors.lastname: Tan
authors.forename: Yvette Y
authors.initials: YY
authors.lastname: Yien
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: D001421:Bacteria, Anaerobic / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D010802:Phylogeny; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013696:Temperature; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000516:alpha-Amylases