Intermolecular correlations are necessary to explain diffuse scattering from protein crystals

IUCrJ
Ariana PeckThomas J Lane

Abstract

Conformational changes drive protein function, including catalysis, allostery and signaling. X-ray diffuse scattering from protein crystals has frequently been cited as a probe of these correlated motions, with significant potential to advance our understanding of biological dynamics. However, recent work has challenged this prevailing view, suggesting instead that diffuse scattering primarily originates from rigid-body motions and could therefore be applied to improve structure determination. To investigate the nature of the disorder giving rise to diffuse scattering, and thus the potential applications of this signal, a diverse repertoire of disorder models was assessed for its ability to reproduce the diffuse signal reconstructed from three protein crystals. This comparison revealed that multiple models of intramolecular conformational dynamics, including ensemble models inferred from the Bragg data, could not explain the signal. Models of rigid-body or short-range liquid-like motions, in which dynamics are confined to the biological unit, showed modest agreement with the diffuse maps, but were unable to reproduce experimental features indicative of long-range correlations. Extending a model of liquid-like motions to include...Continue Reading

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Citations

Apr 30, 2019·Philosophical Transactions. Series A, Mathematical, Physical, and Engineering Sciences·Andreas FörsterClemens Schulze-Briese
Mar 11, 2020·Nature Communications·Steve P MeisburgerNozomi Ando
May 17, 2018·IUCrJ·Michael E Wall
Feb 20, 2018·Current Opinion in Structural Biology·Michael E WallJames S Fraser
Jul 23, 2021·Biochemistry·Da XuNozomi Ando

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Methods Mentioned

BETA
X-ray
total protein scattering

Software Mentioned

DIALS
XDS
PHENIX
REFMAC
Coot
Thor
Phaser

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