Tracking Flavin Conformations in Protein Crystal Structures with Raman Spectroscopy and QM/MM Calculations

Abstract

Damaged goods? Detailed knowledge of the cofactor conformation is essential for the functional analysis of flavoenzyme crystal structures. However, photoelectrons generated by X-rays during crystal-data collection can reduce the flavin cofactor and thus change its geometry (see picture). Monitoring of the flavin vibrational modes by Raman spectroscopy during X-ray crystal-data collection provided important information on the actual flavin state. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.