ArticleActa crystallographica. Section D, Biological crystallography2011
High-resolution neutron crystallographic studies of the hydration of the coenzyme cob(II)alamin.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Ultrafast X-ray Absorption Spectroscopy Reveals Excited-State Dynamics of BThe journal of physical chemistry. B · 2024Article
- Efficient data reduction for time-of-flight neutron scattering experiments on single crystals.Journal of applied crystallography · 2022Article
- Controlling inversion disorder in a stoichiometric spinel magnet.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Direct air capture of CO-IUCrJ · 2019Article
- Improving the accuracy and resolution of neutron crystallographic data by three-dimensional profile fitting of Bragg peaks in reciprocal space.Acta crystallographica. Section D, Structural biology · 2018Article
- SENJU: a new time-of-flight single-crystal neutron diffractometer at J-PARC.Journal of applied crystallography · 2016Article
- An improved method for calibrating time-of-flight Laue single-crystal neutron diffractometers.Journal of applied crystallography · 2014Article
- Seeing the chemistry in biology with neutron crystallography.Physical chemistry chemical physics : PCCP · 2013Article
- Article
- Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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9 authors.
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Abstract
The hydration of the coenzyme cob(II)alamin has been studied using high-resolution monochromatic neutron crystallographic data collected at room temperature to a resolution of 0.92 Å on the original D19 diffractometer with a prototype 4° × 64° detector at the high-flux reactor neutron source run by the Institute Laue-Langevin. The resulting structure provides hydrogen-bonding parameters for the hydration of biomacromolecules to unprecedented accuracy. These experimental parameters will be used to define more accurate force fields for biomacromolecular structure refinement. The presence of a hydrophobic bowl motif surrounded by flexible side chains with terminal functional groups may be significant for the efficient scavenging of ligands. The feasibility of extending the resolution of this structure to ultrahigh resolution was investigated by collecting time-of-flight neutron crystallographic data during commissioning of the TOPAZ diffractometer with a prototype array of 14 modular 2° × 21° detectors at the Spallation Neutron Source run by Oak Ridge National Laboratory.
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