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Related Experiment Video

Updated: May 16, 2025

Virtual Hand with Ambiguous Movement between the Self and Other Origin: Sense of Ownership and 'Other-Produced' Agency
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If you cannot see it, is it still there?

Lukas Leitner1, Jesse Hudspeth2,1, Sebastiaan Werten3

  • 1Institute of Genetic Epidemiology Medical University of Innsbruck Schöpfstrasse 41 6020Innsbruck Austria.

Journal of Applied Crystallography
|April 2, 2025
PubMed
Summary
This summary is machine-generated.

Ensemble refinement visualizes flexible protein regions often missed in crystallography. This method reveals the dynamic conformational landscape of

Keywords:
ensemble refinementflexibilityinvisible protein segmentsmissing electron densitymodellingprotein crystallography

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Computational Biology

Background:

  • Protein crystallographers use electron density maps to build atomic models.
  • Flexible protein regions are often not visible in electron density maps and are omitted from models.
  • This omission can obscure functionally important protein dynamics.

Purpose of the Study:

  • To demonstrate ensemble refinement as a method for visualizing and analyzing flexible protein segments.
  • To explore the functional implications of molecular flexibility in protein structures.

Main Methods:

  • Applied ensemble refinement to multiple crystal forms of fungal methyl-transferase PsiM.
  • Analyzed the conformational landscape of 'invisible' protein segments.

Main Results:

  • Successfully visualized the dynamic nature of a key substrate recognition loop in PsiM.
  • Illustrated the potential role of this loop's flexibility in substrate binding and release.

Conclusions:

  • Ensemble refinement effectively visualizes biologically relevant flexible protein regions.
  • This technique is a powerful tool for exploring molecular plasticity and modeling dynamic protein components.