Highly constrained multiple-copy refinement of protein crystal structures.
In the course of refining atomic protein structures, one often encounters difficulty with molecules that are unusually flexible or otherwise disordered. We approach the problem by combining two relatively recent developments: simultaneous refinement of multiple protein conformations and highly constrained refinement. A constrained Langevin dynamics refinement is tested on two proteins: neurotrophin-3 and glutamine synthetase. The method produces closer agreement between the calculated and observed scattering amplitudes than standard, single-copy, Gaussian atomic displacement parameter refinement. This is accomplished without significantly increasing the number of fitting parameters in the model. These results suggest that loop motion in proteins within a crystal lattice can be extensive and that it is poorly modeled by isotropic Gaussian distributions for each atom.
Pellegrini
M
M
Molecular Biology Institute, University of California, Los Angeles 90095-1570, USA.
Grønbech-Jensen
N
N
Kelly
J A
JA
Pfluegl
G M
GM
Yeates
T O
TO
D000818:Animals; D003198:Computer Simulation; D018360:Crystallography, X-Ray / Q000379:methods*; D005974:Glutamate-Ammonia Ligase / Q000737:chemistry; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D009414:Nerve Growth Factors / Q000737:chemistry; D020933:Neurotrophin 3; D016011:Normal Distribution; D011487:Protein Conformation
D009414:Nerve Growth Factors; D020933:Neurotrophin 3; D005974:Glutamate-Ammonia Ligase