WikiSysop: Created page with "== Citation == Thibodeaux, A., Bu, G., Edwards, L.C. and Rova Danelius, E. 2026. High-throughput automated molecular replacement for small-molecule MicroED data. IUCrJ. 13, 3 (2026). == Abstract == Interest in electron diffraction (ED) for structural characterization of both proteins and small molecules has grown significantly over the last decade. While ab initio phasing methods remain the gold standard for ED data from smallmolecule samples, radiation beam damage du..."

2026-05-13T05:45:10Z

Created page with "== Citation == Thibodeaux, A., Bu, G., Edwards, L.C. and Rova Danelius, E. 2026. High-throughput automated molecular replacement for small-molecule MicroED data. IUCrJ. 13, 3 (2026). == Abstract == Interest in electron diffraction (ED) for structural characterization of both proteins and small molecules has grown significantly over the last decade. While ab initio phasing methods remain the gold standard for ED data from smallmolecule samples, radiation beam damage du..."

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== Citation ==

Thibodeaux, A., Bu, G., Edwards, L.C. and Rova Danelius, E. 2026. High-throughput automated molecular replacement for small-molecule MicroED data. IUCrJ. 13, 3 (2026).

== Abstract ==

Interest in electron diffraction (ED) for structural characterization of both
proteins and small molecules has grown significantly over the last decade. While
ab initio phasing methods remain the gold standard for ED data from smallmolecule
samples, radiation beam damage during data collection and poor
crystallinity of the nanocrystalline sample can make this method unfeasible –
particularly for challenging molecules that exhibit conformational flexibility.
Molecular replacement (MR) is the most commonly used phasing method for
protein ED data and can circumnavigate issues related to diminished data
quality. However, its application to small molecules has been limited due to the
lack of methods for generating optimal trial conformations. Herein, a high-throughput
automated molecular replacement workflow has been developed to
solve a novel ED structure of corilagin, a macrocyclic gallotannin with pharmaceutical
relevance, which could not be solved with ab initio phasing. The
method was validated against three similar macrocycles with known structures
(paritaprevir-, paritaprevir- and grazoprevir) at varying data resolution limits
(1.0, 1.2, 1.4, 1.5, 1.6, 1.8 and 2.0 A ˚ ). At all these resolutions for all three
structures, the developed workflow was successful and produced solutions with
R factors and RMSD values within acceptable limits of the ab initio solved
structure.

== Keywords ==

== Links ==

https://journals.iucr.org/paper?vq5007

== Related software ==

== Related methods ==

== Comments ==

2026Thibodeaux MR - Revision history