Crystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii
Li, N. Patel, B.K.C. Mijts, B.N. Swaminathan, K.
Patel, B.K.C.
Mijts, B.N.
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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.
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Source Title
Acta Crystallographica Section D: Biological Crystallography
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Date
2002-12-01
DOI
10.1107/S0907444902015469
Type
Article