Please use this identifier to cite or link to this item:
|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|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Apr 4, 2020
WEB OF SCIENCETM
checked on Mar 19, 2020
checked on Mar 28, 2020
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.