Authors: Schirò A, Carlon A, Parigi G, Murshudov G, Calderone V, Ravera E, Luchinat C
Abstract
X-ray crystallography and NMR contain complementary information for the structural characterization of biological macromolecules. X-ray diffraction is primarily sensitive to the overall shape of the molecule, whereas NMR is mostly sensitive to the atomic detail. Their combination can therefore provide a stronger justification for the resulting structure. For their combination we have recently proposed REFMAC-NMR, which relies on primary data from both techniques for joint refinement. This possibility raises the compelling question of how far the complementarity can be extended. In this paper, we describe an integrative approach to the refinement with NMR data of four X-ray structures of hen-egg-white lysozyme, solved at atomic resolution in four different crystal forms, and we demonstrate that the outcome critically depends on the crystal form itself, reflecting the sensitivity of NMR to fine details.
[NMR paper] Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
Related Articles Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
J Struct Biol. 2015 Jul 20;
Authors: Vögeli B, Olsson S, Riek R, Güntert P
Abstract
The study of the spatial sampling of biomolecules is essential to understanding the structure-dynamics-function relationship. We have established a protocol for the determination of...
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07-25-2015 01:54 PM
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics
Publication date: Available online 20 July 2015
Source:Journal of Structural Biology</br>
Author(s): Beat Vögeli, Simon Olsson, Roland Riek, Peter Güntert</br>
The study of the spatial sampling of biomolecules is essential to understanding the structure-dynamics-function relationship. We have established a protocol for the determination of multiple-state ensembles based on exact measurements of the nuclear Overhauser effect (eNOE). The...
[NMR analysis blog] Mnova 6.0, at last! GSD, Line Fitting, Data Analysis, handling of LC/GC/MS data and m
Mnova 6.0, at last! GSD, Line Fitting, Data Analysis, handling of LC/GC/MS data and much more!
It's been over 6 weeks since my last post on this blog but don’t worry, I haven’t been idle. On the contrary, I have a very good excuse for this lack of posts: We all at Mestrelab have been working very hard trying to get version 6.0 of Mnova finished. Now I’m delighted to announce that we have done it and version 6.0 is finally available for download from our Web site. This is certainly a major upgrade of the software in which we have put a lot of work and passion. It brings a number of...
On the complementarity of X-ray and NMR data.
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