A quick solution: ab initio structure determination of a 19 kDa metalloproteinase using ACORN.
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.
McAuley
K E
KE
York Structural Biology Laboratory, Chemistry Department, University of York, Heslington, York YO10 5DD, England.
Jia-Xing
Y
Y
Dodson
E J
EJ
Lehmbeck
J
J
Østergaard
P R
PR
Wilson
K S
KS
D001236:Aspergillus oryzae / Q000201:enzymology*; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D008666:Metalloendopeptidases / Q000737:chemistry*; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D012984:Software
D008666:Metalloendopeptidases; C070788:neutral protease II, Aspergillus oryzae