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-Structure paper
Title | Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions. |
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Journal, issue, pages | Appl. Microbiol. Biotechnol., Vol. 99, Page 7973-7986, Year 2015 |
Publish date | Sep 3, 2014 (structure data deposition date) |
Authors | Feng, J. / Wang, L. / Liu, H. / Yang, X. / Liu, L. / Xie, Y. / Liu, M. / Zhao, Y. / Li, X. / Wang, D. ...Feng, J. / Wang, L. / Liu, H. / Yang, X. / Liu, L. / Xie, Y. / Liu, M. / Zhao, Y. / Li, X. / Wang, D. / Zhan, C.G. / Liao, F. |
External links | Appl. Microbiol. Biotechnol. / PubMed:25786739 |
Methods | X-ray diffraction |
Resolution | 1.401 - 1.8 Å |
Structure data | PDB-4r8x: PDB-4r99: |
Chemicals | ChemComp-HOH: ChemComp-SO4: |
Source |
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Keywords | HYDROLASE / Bacillus fastidious uricase / fold / stability |