Heme peroxidase—Trapping intermediates by cryo neutron crystallography

Hanna Kwon*, Tobias E. Schrader, Andreas Ostermann, Matthew P. Blakeley, Emma L. Raven, Peter C.E. Moody

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter in a book

4 Citations (Scopus)

Abstract

By combining the normal practice for X-ray crystallography of collecting diffraction data at 100 K 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.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherElsevier Academic Press Inc
Pages379-389
Number of pages11
DOIs
Publication statusPublished - 2020

Publication series

NameMethods in Enzymology
Volume634
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Cryo-trapping
  • Enzyme intermediate
  • Heme peroxidase
  • Neutron diffraction
  • Protonation state

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