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dc.contributor.authorLi, Nan
dc.contributor.authorPatel, Bharat
dc.contributor.authorMijts, Benjamin
dc.contributor.authorSwaminathan, Kunchithapadam
dc.date.accessioned2017-05-03T11:40:28Z
dc.date.available2017-05-03T11:40:28Z
dc.date.issued2002
dc.date.modified2009-09-16T07:42:19Z
dc.identifier.issn09074449
dc.identifier.doi10.1107/S0907444902015469
dc.identifier.urihttp://hdl.handle.net/10072/6971
dc.description.abstractThis report is the first crystallographic study of an amylase from an organism that is both thermophilic and halophilic. -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 Ŭ using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.89 Ů
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBlackwell Munksgaard
dc.publisher.placeDenmark
dc.publisher.urihttp://www.iucr.org/
dc.relation.ispartofpagefrom2125
dc.relation.ispartofpageto2126
dc.relation.ispartofjournalActa Crystallographica Section D Biological Crystallography
dc.relation.ispartofvolumeD58
dc.subject.fieldofresearchHistory and Archaeology
dc.subject.fieldofresearchPhysical Sciences
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchcode21
dc.subject.fieldofresearchcode02
dc.subject.fieldofresearchcode03
dc.subject.fieldofresearchcode06
dc.titleCrystallization of an α-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2002
gro.hasfulltextNo Full Text
gro.griffith.authorPatel, Bharat K.
gro.griffith.authorMijts, Benjamin


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