Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444902015469
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dc.titleCrystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii
dc.contributor.authorLi, N.
dc.contributor.authorPatel, B.K.C.
dc.contributor.authorMijts, B.N.
dc.contributor.authorSwaminathan, K.
dc.date.accessioned2014-10-27T08:25:12Z
dc.date.available2014-10-27T08:25:12Z
dc.date.issued2002-12-01
dc.identifier.citationLi, 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
dc.identifier.issn09074449
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100379
dc.description.abstractThis 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1107/S0907444902015469
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1107/S0907444902015469
dc.description.sourcetitleActa Crystallographica Section D: Biological Crystallography
dc.description.volume58
dc.description.issue12
dc.description.page2125-2126
dc.description.codenABCRE
dc.identifier.isiut000179468800023
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