Determination and refinement of the canine parvovirus empty‐capsid structure

Determination and refinement of the canine parvovirus empty‐capsid structure The canine parvovirus (CPV) empty‐capsid structure has been determined and refined to 3.0 Å resolution in the tetragonal space group P43212 with cell dimensions a = b = 254.5 and c = 795.0 Å. The successful structure determination shows that reasonably good diffraction data were obtained in spite of the very long c axis. The structure was solved by molecular replacement using the electron density of CPV full particles in a monoclinic space group. The phases were refined by non‐crystallographic symmetry averaging. The structure refinement was carried out by using the programs PROLSQ and X‐PLOR. The final R factor for the structure that included 85 water molecules per icosahedral asymmetric unit was 21.1% for reflections between 6.0 and 3.0 Å resolution with an r.m.s. deviation of bond lengths of 0.020 Å from ideal values. The structure of CPV empty capsids showed conformational differences with respect to full capsids at a region where icosahedrally ordered DNA in full particles interacts with the capsid protein. It also confirmed the absence of density along the fivefold axis in the CPV empty‐particle structure in contrast to the situation in CPV full particles. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Determination and refinement of the canine parvovirus empty‐capsid structure

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Publisher
Wiley
Copyright
Copyright © 1993 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
D.O.I.
10.1107/S0907444993006870
Publisher site
See Article on Publisher Site

Abstract

The canine parvovirus (CPV) empty‐capsid structure has been determined and refined to 3.0 Å resolution in the tetragonal space group P43212 with cell dimensions a = b = 254.5 and c = 795.0 Å. The successful structure determination shows that reasonably good diffraction data were obtained in spite of the very long c axis. The structure was solved by molecular replacement using the electron density of CPV full particles in a monoclinic space group. The phases were refined by non‐crystallographic symmetry averaging. The structure refinement was carried out by using the programs PROLSQ and X‐PLOR. The final R factor for the structure that included 85 water molecules per icosahedral asymmetric unit was 21.1% for reflections between 6.0 and 3.0 Å resolution with an r.m.s. deviation of bond lengths of 0.020 Å from ideal values. The structure of CPV empty capsids showed conformational differences with respect to full capsids at a region where icosahedrally ordered DNA in full particles interacts with the capsid protein. It also confirmed the absence of density along the fivefold axis in the CPV empty‐particle structure in contrast to the situation in CPV full particles.

Journal

Acta Crystallographica Section DWiley

Published: Nov 1, 1993

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