Refinement of protein structures using a combination of quantum-mechanical calculations with neutron and X-ray crystallographic data

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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.


Enheter & grupper
Externa organisationer
  • European Spallation Source ESS AB

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi


Sidor (från-till)368-380
Antal sidor13
TidskriftActa Crystallographica Section D: Structural Biology
StatusPublished - 2019
Peer review utfördJa


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