The α-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis
✍ Scribed by Stefan Strobl; Franz-Xaver Gomis-Rüth; Klaus Maskos; Gerhard Frank; Robert Huber; Rudi Glockshuber
- Book ID
- 117107585
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 674 KB
- Volume
- 409
- Category
- Article
- ISSN
- 0014-5793
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## Abstract A cold‐active α‐amylase was purified from culture supernatants of the antarctic psychrophile __Alteromonas haloplanctis__ A23 grown at 4 °C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold‐adapted enzyme have
The results of X-ray diffraction analyses on two m-aminoisobutyric acid (Aibl derivativcs, methyl u-(acetylamino)isobuknoate (Ac-Aib-OMc. I ) and bcnzyl a-[(beazyloxycarbonyl)arnino]isobutanoate (2-Aib-OBA, 2), and two terminally blocked, Aib-conlining dipcptides, methyl cr-[(acctyl-~-alanyl)nmino]i