Crystallization of an α-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, α-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 P212121, with unit-cell parameters a = 55.126, b = 61.658, c = 147.625 Å, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.89 Å.