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Diffuse X-ray Scattering from Correlated Motions in a Protein Crystal

https://doi.org/10.1101/805424
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/prot.21246openalex-snapshot
Protein dynamics from X‐ray crystallography: Anisotropic, global motion in diffuse scattering patterns
inferredcites →https://doi.org/10.1002/prot.340120208openalex-snapshot
Correlations of atomic movements in lysozyme crystals
inferredcites →https://doi.org/10.1002/wcms.1402openalex-snapshot
Molecular dynamics simulations of macromolecular crystals
inferredcites →https://doi.org/10.1006/jmbi.1998.1754openalex-snapshot
X-ray diffuse scattering and rigid-body motion in crystalline lysozyme probed by molecular dynamics simulation 1 1Edited by R. Huber
inferredcites →https://doi.org/10.1016/0079-6107(85)90002-1openalex-snapshot
Mapping protein dynamics by X-ray diffraction
inferredcites →https://doi.org/10.1016/j.bpj.2010.08.013openalex-snapshot
Evaluating Elastic Network Models of Crystalline Biological Molecules with Temperature Factors, Correlated Motions, and Diffuse X-Ray Scattering
inferredcites →https://doi.org/10.1016/j.sbi.2014.07.005openalex-snapshot
E pluribus unum, no more: from one crystal, many conformations
inferredcites →https://doi.org/10.1016/j.sbi.2018.01.009openalex-snapshot
Bringing diffuse X-ray scattering into focus
inferredcites →https://doi.org/10.1016/j.str.2009.08.015openalex-snapshot
On the Relationship between Diffraction Patterns and Motions in Macromolecular Crystals
inferredcites →https://doi.org/10.1016/s0006-3495(03)74738-9openalex-snapshot
Sound Velocity and Elasticity of Tetragonal Lysozyme Crystals by Brillouin Spectroscopy
inferredcites →https://doi.org/10.1016/s0009-2614(00)01267-7openalex-snapshot
Sound velocity and dynamic elastic constants of lysozyme single crystals
inferredcites →https://doi.org/10.1016/s0969-2126(97)00308-0openalex-snapshot
Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering
inferredcites →https://doi.org/10.1021/acs.accounts.6b00562openalex-snapshot
Correlated Motions from Crystallography beyond Diffraction
inferredcites →https://doi.org/10.1021/acs.chemrev.6b00790openalex-snapshot
X-ray Scattering Studies of Protein Structural Dynamics
inferredcites →https://doi.org/10.1021/j100315a002openalex-snapshot
Interpretation of atomic displacement parameters from diffraction studies of crystals
inferredcites →https://doi.org/10.1038/262325a0openalex-snapshot
The hinge-bending mode in lysozyme
inferredcites →https://doi.org/10.1038/332659a0openalex-snapshot
Liquid-like movements in crystalline insulin
inferredcites →https://doi.org/10.1038/nature16949openalex-snapshot
Macromolecular diffractive imaging using imperfect crystals
inferredcites →https://doi.org/10.1038/nsb0294-124openalex-snapshot
Correlated intramolecular motions and diffuse x–ray scattering in lysozyme
inferredcites →https://doi.org/10.1063/1.3051547openalex-snapshot
X-Ray Diffraction in Crystals, Imperfect Crystals, and Amorphous Bodies
inferredcites →https://doi.org/10.1073/pnas.1416744111openalex-snapshot
Conformational dynamics of a crystalline protein from microsecond-scale molecular dynamics simulations and diffuse X-ray scattering
inferredcites →https://doi.org/10.1073/pnas.1524048113openalex-snapshot
Measuring and modeling diffuse scattering in protein X-ray crystallography
inferredcites →https://doi.org/10.1073/pnas.82.15.4995openalex-snapshot
Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme.
inferredcites →https://doi.org/10.1073/pnas.94.12.6180openalex-snapshot
Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease
inferredcites →https://doi.org/10.1080/0889311x.2015.1046853openalex-snapshot
One hundred years of diffuse scattering
inferredcites →https://doi.org/10.1103/physreve.79.061917openalex-snapshot
Elastic constants in tetragonal hen egg-white lysozyme crystals containing large amount of water
inferredcites →https://doi.org/10.1103/physrevlett.77.1905openalex-snapshot
Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis
inferredcites →https://doi.org/10.1103/physrevlett.79.3090openalex-snapshot
Gaussian Dynamics of Folded Proteins
inferredcites →https://doi.org/10.1103/physrevlett.95.218103openalex-snapshot
Correlated Dynamics Determining X-Ray Diffuse Scattering from a Crystalline Protein Revealed by Molecular Dynamics Simulation
inferredcites →https://doi.org/10.1103/physrevlett.99.138101openalex-snapshot
Lattice Dynamics of a Protein Crystal
inferredcites →https://doi.org/10.1107/97809553602060000102openalex-snapshot
International Tables for Crystallography
inferredcites →https://doi.org/10.1107/97809553602060000113openalex-snapshot
International Tables for Crystallography
inferredcites →https://doi.org/10.1107/s0108767389012912openalex-snapshot
Thermal motion in protein crystals estimated using laser-generated ultrasound and Young's modulus measurements
inferredcites →https://doi.org/10.1107/s0108768191004585openalex-snapshot
The variety of X-ray diffuse scattering from macromolecular crystals and its respective components
inferredcites →https://doi.org/10.1107/s0365110x56002655openalex-snapshot
A method for converting experimental X-ray intensities to an absolute scale
inferredcites →https://doi.org/10.1107/s0365110x57001085openalex-snapshot
The Fourier transform method for normalizing intensities
inferredcites →https://doi.org/10.1107/s0907444906005270openalex-snapshot
Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
inferredcites →https://doi.org/10.1107/s0907444996002594openalex-snapshot
Molecular Rigid-Body Displacements in a Tetragonal Lysozyme Crystal Confirmed by X-ray Diffuse Scattering
inferredcites →https://doi.org/10.1107/s0907444997013656openalex-snapshot
Refinement of Triclinic Hen Egg-White Lysozyme at Atomic Resolution
inferredcites →https://doi.org/10.1107/s0907444998001875openalex-snapshot
A Description of Imperfections in Protein Crystals
inferredcites →https://doi.org/10.1107/s1399004715013838openalex-snapshot
Acoustic vibrations contribute to the diffuse scatter produced by ribosome crystals
inferredcites →https://doi.org/10.1107/s2052252518000519openalex-snapshot
Internal protein motions in molecular-dynamics simulations of Bragg and diffuse X-ray scattering
inferredcites →https://doi.org/10.1107/s2052252518001124openalex-snapshot
Intermolecular correlations are necessary to explain diffuse scattering from protein crystals
inferredcites →https://doi.org/10.1107/s2052252519000927openalex-snapshot
Rigid-body motion is the main source of diffuse scattering in protein crystallography
inferredcites →https://doi.org/10.1126/science.1218231openalex-snapshot
Linking Crystallographic Model and Data Quality

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1038/s41467-023-36734-3openalex-snapshot
Robust total X-ray scattering workflow to study correlated motion of proteins in crystals
inferred← citeshttps://doi.org/10.1063/4.0000087openalex-snapshot
Reproducibility of protein x-ray diffuse scattering and potential utility for modeling atomic displacement parameters
inferred← citeshttps://doi.org/10.1101/2021.02.11.429988openalex-snapshot
Understanding conformational dynamics from macromolecular crystal diffuse scattering
inferred← citeshttps://doi.org/10.1107/s2059798322011871openalex-snapshot
Molecular-dynamics simulation methods for macromolecular crystallography
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