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|Title:||Crystallization of a novel α-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii||Authors:||Tan, T.-C.
|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|
|Appears in Collections:||Staff Publications|
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