Work

If you cannot see it, is it still there?

Year: 2025

Type: article

Abstract: Protein crystallographers rely on electron density to build atomic models of molecular structures, yet flexible regions often remain unseen in electron density and are omitted. We suggest that ensemble refinement can be used to visualize and analyse the conformational landscape of such 'invisible' protein segments, which is particularly useful in cases where molecular flexibility plays a functional role. Using ensemble refinement on multiple crystal forms of the fungal methyl-transferase PsiM as an example, we illustrate the dynamic nature of a key substrate recognition loop, demonstrating its potential role in substrate binding and release. Ensemble refinement provides a persuasive visualization of biologically relevant flexible regions and can be a powerful tool for exploring molecular plasticity and aiding the modelling of dynamic protein components.

Source: Journal of Applied Crystallography

DOI: 10.1107/s160057672500130x

Authors: Lukas Leitner, Jesse Hudspeth, Sebastiaan Werten, Bernhard Rupp

Institutions: Innsbruck Medical University, Universität Innsbruck, University of Colorado Anschutz

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $5,110

Funder: Austrian Science Fund