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|Title:||Crystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii|
|Authors:||Li, N. |
|Citation:||Li, N., Patel, B.K.C., Mijts, B.N., Swaminathan, K. (2002-12-01). Crystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Acta Crystallographica Section D: Biological Crystallography 58 (12) : 2125-2126. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444902015469|
|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.|
|Source Title:||Acta Crystallographica Section D: Biological Crystallography|
|Appears in Collections:||Staff Publications|
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