Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A data set from the metalloproteinase deuterolysin was collected at atomic resolution (1.0 A) with synchrotron radiation. The high resolution allowed the structure to be solved with the new direct-methods program ACORN using the coordinates of the Zn atom as a starting point. The phases obtained from ACORN were of sufficient quality to allow automated building to be carried out in ARP/wARP. Minimal manual rebuilding of the model was required and the structure determination was completed using the maximum-likelihood refinement program REFMAC. The whole process, starting from the processed and merged data and ending with a refined model, required less than 6 h of computational time.
A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN.,McAuley KE, Jia-Xing Y, Dodson EJ, Lehmbeck J, Ostergaard PR, Wilson KS Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1571-8. Epub 2001, Oct 25. PMID:11679721[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McAuley KE, Jia-Xing Y, Dodson EJ, Lehmbeck J, Ostergaard PR, Wilson KS. A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1571-8. Epub 2001, Oct 25. PMID:11679721
