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
Hauptverfasser: Kwon, Hanna, Schrader, Tobias E, Ostermann, Andreas, Blakeley, Matthew P, Raven, Emma L, Moody, Peter C E
Format: Artikel
Sprache:eng
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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.
ISSN:1557-7988
DOI:10.1016/bs.mie.2020.01.010