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Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43890213" target="_blank" >RIV/60076658:12310/15:43890213 - isvavai.cz</a>

  • Alternative codes found

    RIV/67179843:_____/15:00452881

  • Result on the web

    <a href="http://scripts.iucr.org/cgi-bin/paper?S2053230X15020270" target="_blank" >http://scripts.iucr.org/cgi-bin/paper?S2053230X15020270</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S2053230X15020270" target="_blank" >10.1107/S2053230X15020270</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum

  • Original language description

    The glyceraldehyde dehydrogenase from Thermoplasma acidophilum (TaAlDH) is a microbial enzyme that catalyzes the oxidation of D-glyceraldehyde to D-glycerate in the artificial enzyme cascade designed for the conversion of glucose to the organic solventsisobutanol and ethanol. Various mutants of TaAlDH were constructed by a random approach followed by site-directed and saturation mutagenesis in order to improve the properties of the enzyme that are essential for its functioning within the cascade. Two enzyme variants, wild-type TaAlDH (TaAlDHwt) and an F34M+S405N variant (TaAlDH F34M+S405N), were successfully crystallized. Crystals of TaAlDHwt belonged to the monoclinic space group P1211 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 angstrom. TaAlDH F34M+S405N crystallized in two different space groups: triclinic P1 with 16 molecules per asymmetric unit and monoclinic C121 with four molecules per asymmetric unit. These crystals diffracted to resolution

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Acta Crystallographica Section F-Structural Biology and Communications

  • ISSN

    2053-230X

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    DEC 2015

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    6

  • Pages from-to

    1475-1480

  • UT code for WoS article

    000369376500006

  • EID of the result in the Scopus database