Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability

The crystal structure of Bacillus amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. The final model of BAA is composed of two molecules in a back-to-back orientation, which is likely to be a consequence of crys...

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Hlavní autoři: Alikhajeh, Jahan, Khajeh, Khosro, Ranjbar, Bijan, Naderi-Manesh, Hossein, Lin, Yi-Hung, Liu, Enhung, Guan, Hong-Hsiang, Hsieh, Yin-Cheng, Chuankhayan, Phimonphan, Huang, Yen-Chieh, Jeyaraman, Jeyakanthan, Liu, Ming-Yih, Chen, Chun-Jung
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2010
Témata:
Structural Communications
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2815676/
https://ncbi.nlm.nih.gov/pubmed/20124706
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309109051938
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