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. doi: 10.1107/s090744490101335x. Epub 2001 Oct 25.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus oryzae / enzymology*
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Metalloendopeptidases / chemistry*
  • Models, Molecular
  • Molecular Weight
  • Protein Conformation
  • Software*

Substances

  • Metalloendopeptidases
  • neutral protease II, Aspergillus oryzae

Associated data

  • PDB/1EB6