Heme peroxidase-Trapping intermediates by cryo neutron crystallography
By combining the normal practice for X-ray crystallography of collecting diffraction data at 100K with neutron crystallography the structures of cryo-trapped enzyme intermediates have been determined, revealing the positions of the previously hidden hydrogens that are essential to a better understan...
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Veröffentlicht in: | Methods in enzymology 2020, Vol.634, p.379-389 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | By combining the normal practice for X-ray crystallography of collecting diffraction data at 100K with neutron crystallography the structures of cryo-trapped enzyme intermediates have been determined, revealing the positions of the previously hidden hydrogens that are essential to a better understanding of the involved mechanism. |
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ISSN: | 1557-7988 |
DOI: | 10.1016/bs.mie.2020.01.010 |