Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444903018754
Title: Crystallization of a novel α-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii
Authors: Tan, T.-C.
Yien, Y.Y.
Patel, B.K.C.
Mijts, B.N.
Swaminathan, K. 
Issue Date: Dec-2003
Citation: Tan, T.-C., Yien, Y.Y., Patel, B.K.C., Mijts, B.N., Swaminathan, K. (2003-12). Crystallization of a novel α-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii. Acta Crystallographica - Section D Biological Crystallography 59 (12) : 2257-2258. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444903018754
Abstract: 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 C2, with unit-cell parameters a = 225.85, b = 77.16, c = 50.13 Å, β = 99.32°, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.97 Å.
Source Title: Acta Crystallographica - Section D Biological Crystallography
URI: http://scholarbank.nus.edu.sg/handle/10635/100378
ISSN: 09074449
DOI: 10.1107/S0907444903018754
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