Crystallization of a novel a-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii

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Tan, Tien-Chye
Y. Yien, Yvette
Patel, Bharat
Mijts, Benjamin
Swaminathan, Kunchithapadam
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C E Bugg

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2003
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This is a report on the structure determination of AmyB, the second a-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-�sidue 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 Ŭ ߠ= 99.32ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-�ys to a resolution limit of 1.97 Ů

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Acta Crystallographica, Section D: Biological Crystallography

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D59

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Physical Sciences

Chemical Sciences

Biological Sciences

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