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Protein Crystallography

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Cover of 'Protein Crystallography'

Table of Contents

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    Book Overview
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    Chapter 1 Expression and Purification of Recombinant Proteins in Escherichia coli with a His6 or Dual His6-MBP Tag
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    Chapter 2 Protein Crystallization
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    Chapter 3 Advanced Methods of Protein Crystallization
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    Chapter 4 The “Sticky Patch” Model of Crystallization and Modification of Proteins for Enhanced Crystallizability
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    Chapter 5 Crystallization of Membrane Proteins: An Overview
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    Chapter 6 Locating and Visualizing Crystals for X-Ray Diffraction Experiments
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    Chapter 7 Collection of X-Ray Diffraction Data from Macromolecular Crystals
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    Chapter 8 Identifying and Overcoming Crystal Pathologies: Disorder and Twinning
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    Chapter 9 Applications of X-Ray Micro-Beam for Data Collection
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    Chapter 10 Serial Synchrotron X-Ray Crystallography (SSX)
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    Chapter 11 Time-Resolved Macromolecular Crystallography at Modern X-Ray Sources
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    Chapter 12 Structure Determination Using X-Ray Free-Electron Laser Pulses
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    Chapter 13 Processing of XFEL Data
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    Chapter 14 Many Ways to Derivatize Macromolecules and Their Crystals for Phasing
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    Chapter 15 Experimental Phasing: Substructure Solution and Density Modification as Implemented in SHELX
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    Chapter 16 Contemporary Use of Anomalous Diffraction in Biomolecular Structure Analysis
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    Chapter 17 Long-Wavelength X-Ray Diffraction and Its Applications in Macromolecular Crystallography
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    Chapter 18 Acknowledging Errors: Advanced Molecular Replacement with Phaser
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    Chapter 19 Rosetta Structure Prediction as a Tool for Solving Difficult Molecular Replacement Problems
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    Chapter 20 Radiation Damage in Macromolecular Crystallography
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    Chapter 21 Boxes of Model Building and Visualization
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    Chapter 22 Structure Refinement at Atomic Resolution
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    Chapter 23 Low Resolution Refinement of Atomic Models Against Crystallographic Data
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    Chapter 24 Stereochemistry and Validation of Macromolecular Structures
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    Chapter 25 Validation of Protein–Ligand Crystal Structure Models: Small Molecule and Peptide Ligands
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    Chapter 26 Protein Data Bank (PDB): The Single Global Macromolecular Structure Archive
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    Chapter 27 Databases, Repositories, and Other Data Resources in Structural Biology
Attention for Chapter 22: Structure Refinement at Atomic Resolution
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Chapter title
Structure Refinement at Atomic Resolution
Chapter number 22
Book title
Protein Crystallography
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-7000-1_22
Pubmed ID
Book ISBNs
978-1-4939-6998-2, 978-1-4939-7000-1
Authors

Mariusz Jaskolski

Editors

Alexander Wlodawer, Zbigniew Dauter, Mariusz Jaskolski

Abstract

X-Ray diffraction data at atomic resolution, i.e., beyond 1.2 Å, provide the most detailed and reliable information we have about the structure of macromolecules, which is especially important for validating new discoveries and resolving subtle issues of molecular mechanisms. Refinement at atomic resolution allows reliable interpretation of static disorder and solvent structure, as well as modeling of anisotropic atomic vibrations and even of H atoms. Stereochemical restraints can be relaxed or removed, providing unbiased information about macromolecular stereochemistry, which in turn can be used to define improved conformation-dependent libraries, and the surplus of data allows estimation of least-squares uncertainties in the derived parameters. At ultrahigh resolution it is possible to study charge density distribution by multipolar refinement of electrons in non-spherical orbitals.

Mendeley readers

The data shown below were compiled from readership statistics for 7 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 7 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 2 29%
Student > Bachelor 1 14%
Professor 1 14%
Researcher 1 14%
Professor > Associate Professor 1 14%
Other 1 14%
Readers by discipline Count As %
Chemistry 2 29%
Agricultural and Biological Sciences 2 29%
Biochemistry, Genetics and Molecular Biology 1 14%
Arts and Humanities 1 14%
Unknown 1 14%