Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

The accurate assignment of cofactors in cryo-electron microscopy maps is crucial in determining protein function. This is particularly true for chlorophylls (Chls), for which small structural differences lead to important functional differences. Recent cryo-electron microscopy structures of Chl-containing protein complexes exemplify the difficulties in distinguishing Chl b and Chl f from Chl a. We use these structures as examples to discuss general issues arising from local resolution differences, properties of electrostatic potential maps, and the chemical environment which must be considered to make accurate assignments. We offer suggestions for how to improve the reliability of such assignments.


Christopher J Gisriel, Jimin Wang, Gary W Brudvig, Donald A Bryant. Opportunities and challenges for assigning cofactors in cryo-EM density maps of chlorophyll-containing proteins. Communications biology. 2020 Jul 30;3(1):408

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 32733087

View Full Text