Acta Cryst. D50:889-899 (1994)

Comparison of Homology Model to the Experimental Structure of a Novel Serine Protease

Mike Carson, Charles E. Bugg,
Lawrence J. DeLucas and Sthanam V.L. Narayana

Abstract

A model structure of the human complement enzyme Factor D was built based on homology with related serine proteases. A molecular replacement solution of the Factor D crystal structure employing the homology model refined without manual intervention to an R-factor of 0.249 with 2.4 A native diffraction data. A multiple isomorphous replacement (MIR) electron density map was subsequently produced, leading to a model refined at 2.0 A resolution to an R-factor of 0.188. A homology model built with commercial modeling software was subjected to the same procedure. Comparisons of the homology models to the final refined MIR structure are presented. Major discrepancies were found in critical active site regions.

Introduction

Methods

Results

Discussion

References

(image & paper in nutshell) (cool molecular replacement figure)