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Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii.

Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Research Abstract Details 

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  • Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Abstract Text:

    nan liNan Li,bharat k c patelBharat K C Patel,benjamin n mijtsBenjamin N Mijts,kunchithapadam swaminathanKunchithapadam Swaminathan,

    This report is the first crystallographic study of an amylase from an organism that is both thermophilic and halophilic. alpha-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 P2(1)2(1)2(1), with unit-cell parameters a = 55.126, b = 61.658, c = 147.625 A, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.89 A.

    Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Publishing Authors By Initials

    n liN Li,bk patelBK Patel,bn mijtsBN Mijts,k swaminathanK Swaminathan,

    For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: amylases: alpha-amylase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: amylases: alpha-amylase research

    PUBMED ID PMID:

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    Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Acta crystallographica. Section D, Biological crys

    VOLUME: 58

    Page Numbers: 2125-6

    Journal Abbreviation: Acta Crystallogr. D Biol. Crys

    ISSN: 0907-4449

    DAY: 23

    MONTH: 11

    YEAR: 2002

    Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9305878

    Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Keywords Mesh Terms:

    KEYWORDS: alpha-Amylase

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii. Information

    Substance Name: alpha-Amylase

    Registry Number: EC 3.2.1.1

    Grant and Affiliation Information for Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii.

    AFFILIATION: Laboratory of X-ray Crystallography, Institute of Molecular and Cell Biology, 30 Medical Drive, National University of Singapore, Singapore 117609, Singapore.

    Country: Denmark

    Denmark Research PublicationDenmark Research Publication

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    MEDLINETA: Acta Crystallogr D Biol Crysta

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    Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii Related Publications

     

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