REFMAC5 for the Refinement of Macromolecular Crystal Structures

Overview

Journal Acta Crystallogr D Biol Crystallogr

Specialty Chemistry

Date 2011 Apr 5

PMID 21460454

Citations 4606

Authors

Garib N Murshudov

Pavol Skubak

Andrey A Lebedev

Navraj S Pannu

Roberto A Steiner

Robert A Nicholls

Martyn D Winn

Fei Long

Alexei A Vagin

Affiliations

Soon will be listed here.

Abstract

This paper describes various components of the macromolecular crystallographic refinement program REFMAC5, which is distributed as part of the CCP4 suite. REFMAC5 utilizes different likelihood functions depending on the diffraction data employed (amplitudes or intensities), the presence of twinning and the availability of SAD/SIRAS experimental diffraction data. To ensure chemical and structural integrity of the refined model, REFMAC5 offers several classes of restraints and choices of model parameterization. Reliable models at resolutions at least as low as 4 Å can be achieved thanks to low-resolution refinement tools such as secondary-structure restraints, restraints to known homologous structures, automatic global and local NCS restraints, `jelly-body' restraints and the use of novel long-range restraints on atomic displacement parameters (ADPs) based on the Kullback-Leibler divergence. REFMAC5 additionally offers TLS parameterization and, when high-resolution data are available, fast refinement of anisotropic ADPs. Refinement in the presence of twinning is performed in a fully automated fashion. REFMAC5 is a flexible and highly optimized refinement package that is ideally suited for refinement across the entire resolution spectrum encountered in macromolecular crystallography.

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