ArticleActa crystallographica. Section D, Structural biology2019
Refinement of protein structures using a combination of quantum-mechanical calculations with neutron and X-ray crystallographic data.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Quantum refinement with electron diffraction and X-ray free-electron laser data: comparative study of ribonucleotide reductase dimetal site.Journal of applied crystallography · 2026Article
- Article
- Exploring ligand dynamics in protein crystal structures with ensemble refinement.Acta crystallographica. Section D, Structural biology · 2021Article
- Refinement of RNA Structures Using Amber Force Fields.Crystals · 2021Article
- Neutron structures ofIUCrJ · 2021Article
- Galectin-Glycan Interactions: Guidelines for Monitoring byChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Quantum refinement with multiple conformations: application to the P-cluster in nitrogenase.Acta crystallographica. Section D, Structural biology · 2020Article
- Computational reconstruction of atomistic protein structures from coarse-grained models.Computational and structural biotechnology journal · 2020Review
- Refinement of protein structures using a combination of quantum-mechanical calculations with neutron and X-ray crystallographic data. Corrigendum.Acta crystallographica. Section D, Structural biology · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
Neutron crystallography is a powerful method to determine the positions of H atoms in macromolecular structures. However, it is sometimes hard to judge what would constitute a chemically reasonable model, and the geometry of H atoms depends more on the surroundings (for example the formation of hydrogen bonds) than heavy atoms, so that the empirical geometry information for the H atoms used to supplement the experimental data is often less accurate. These problems may be reduced by using quantum-mechanical calculations. A method has therefore been developed to combine quantum-mechanical calculations with joint crystallographic refinement against X-ray and neutron data. A first validation of this method is provided by re-refining the structure of the galectin-3 carbohydrate-recognition domain in complex with lactose. The geometry is improved, in particular for water molecules, for which the method leads to better-resolved hydrogen-bonding interactions. The method has also been applied to the active copper site of lytic polysaccharide monooxygenase and shows that the protonation state of the amino-terminal histidine residue can be determined.
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