ArticleActa crystallographica. Section D, Biological crystallography2009
Application of normal-mode refinement to X-ray crystal structures at the lower resolution limit.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Measuring and modeling diffuse scattering in protein X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- PIM: phase integrated method for normal mode analysis of biomolecules in a crystalline environment.Journal of molecular biology · 2013Article
- Normal mode analysis with molecular geometry restraints: bridging molecular mechanics and elastic models.Archives of biochemistry and biophysics · 2011Article
- Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The Max-Inf2/Lorentz Center workshop on New algorithms in macromolecular crystallography and electron microscopy.Acta crystallographica. Section D, Biological crystallography · 2009Article
- Cooperative dynamics of proteins unraveled by network models.Wiley interdisciplinary reviews. Computational molecular scienceArticle
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4 authors.
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Abstract
The structural refinement of large complexes at the lower resolution limit is often difficult and inefficient owing to the limited number of reflections and the frequently high-level structural flexibility. A new normal-mode-based X-ray crystallographic refinement method has recently been developed that enables anisotropic B-factor refinement using a drastically smaller number of thermal parameters than even isotropic refinement. Here, the method has been systematically tested on a total of eight systems in the resolution range 3.0-3.9 A. This series of tests established the most applicable scenarios for the method, the detailed procedures for its application and the degree of structural improvement. The results demonstrated substantial model improvement at the lower resolution limit, especially in cases in which other methods such as the translation-libration-screw (TLS) model were not applicable owing to the poorly converged isotropic B-factor distribution. It is expected that this normal-mode-based method will be a useful tool for structural refinement, in particular at the lower resolution limit, in the field of X-ray crystallography.
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