Crystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii

This is a report on the structure determination of AmyB, the second α-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 C 2, with unit-cell parameters a = 225.85, b = 77.16, c = 50.13 A, β = 99.32°, using the hanging-drop vapour-diffusion method. The crystal diffracts X-­rays to a resolution limit of 1.97 A.