Work

Symmetry Breaking under Vectorial Perturbations in Macromolecular X-ray Crystallography

Year: 2026

Type: preprint

Abstract: Proteins are molecular machines whose dynamics govern their function. Using time-resolved crystallography, the basis of protein mechanics can be uncovered by physical perturbation on protein crystals. Perturbations are often vector fields that, in crystals, break symmetry. Lacking existing tools for analyzing symmetry breaking, we built open-source software to do so. We applied this method to three time-resolved crystallography experiments and analyzed the effect of vectorial perturbations on macromolecular crystal structure. We demonstrate that our method can handle symmetry reduction in all 65 Sohncke space groups.

Source: bioRxiv (Cold Spring Harbor Laboratory)

DOI: 10.64898/2026.09.28.753211

Authors: Harrison K. Wang, Jack B. Greisman, Kevin M. Dalton, Rick A. Hewitt, K. Ian White, Doeke R. Hekstra

Institutions: Harvard University, D. E. Shaw Research, SLAC National Accelerator Laboratory, Linac Coherent Light Source, New York University, Howard Hughes Medical Institute, Stanford University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: BioCARS: Structural Dynamics and Biological Mechanisms, Identifying Principles of Protein Mechanics by Applying Force and Observing Motion, Center for Biomolecular Structure (CBMS)

OpenAlex ID: W7214964035

Cites: 46

Cited by:

Related to: 10