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Protein Crystallography

Overview of attention for book
Cover of 'Protein Crystallography'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Expression and Purification of Recombinant Proteins in Escherichia coli with a His6 or Dual His6-MBP Tag
  3. Altmetric Badge
    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
  28. Altmetric Badge
    Chapter 27 Databases, Repositories, and Other Data Resources in Structural Biology
Attention for Chapter 4: The “Sticky Patch” Model of Crystallization and Modification of Proteins for Enhanced Crystallizability
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Chapter title
The “Sticky Patch” Model of Crystallization and Modification of Proteins for Enhanced Crystallizability
Chapter number 4
Book title
Protein Crystallography
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-7000-1_4
Pubmed ID
Book ISBNs
978-1-4939-6998-2, 978-1-4939-7000-1
Authors

Zygmunt S. Derewenda, Adam Godzik, Derewenda, Zygmunt S., Godzik, Adam

Editors

Alexander Wlodawer, Zbigniew Dauter, Mariusz Jaskolski

Abstract

Crystallization of macromolecules has long been perceived as a stochastic process, which cannot be predicted or controlled. This is consistent with another popular notion that the interactions of molecules within the crystal, i.e., crystal contacts, are essentially random and devoid of specific physicochemical features. In contrast, functionally relevant surfaces, such as oligomerization interfaces and specific protein-protein interaction sites, are under evolutionary pressures so their amino acid composition, structure, and topology are distinct. However, current theoretical and experimental studies are significantly changing our understanding of the nature of crystallization. The increasingly popular "sticky patch" model, derived from soft matter physics, describes crystallization as a process driven by interactions between select, specific surface patches, with properties thermodynamically favorable for cohesive interactions. Independent support for this model comes from various sources including structural studies and bioinformatics. Proteins that are recalcitrant to crystallization can be modified for enhanced crystallizability through chemical or mutational modification of their surface to effectively engineer "sticky patches" which would drive crystallization. Here, we discuss the current state of knowledge of the relationship between the microscopic properties of the target macromolecule and its crystallizability, focusing on the "sticky patch" model. We discuss state-of-the-art in silico methods that evaluate the propensity of a given target protein to form crystals based on these relationships, with the objective to design variants with modified molecular surface properties and enhanced crystallization propensity. We illustrate this discussion with specific cases where these approaches allowed to generate crystals suitable for structural analysis.

Twitter Demographics

The data shown below were collected from the profiles of 3 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 15 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 15 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 5 33%
Student > Bachelor 2 13%
Researcher 2 13%
Librarian 1 7%
Student > Master 1 7%
Other 0 0%
Unknown 4 27%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 27%
Chemistry 3 20%
Computer Science 2 13%
Earth and Planetary Sciences 1 7%
Agricultural and Biological Sciences 1 7%
Other 0 0%
Unknown 4 27%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 November 2018.
All research outputs
#11,676,753
of 15,298,914 outputs
Outputs from Methods in molecular biology
#4,014
of 8,989 outputs
Outputs of similar age
#182,479
of 271,218 outputs
Outputs of similar age from Methods in molecular biology
#9
of 23 outputs
Altmetric has tracked 15,298,914 research outputs across all sources so far. This one is in the 20th percentile – i.e., 20% of other outputs scored the same or lower than it.
So far Altmetric has tracked 8,989 research outputs from this source. They receive a mean Attention Score of 2.6. This one is in the 48th percentile – i.e., 48% of its peers scored the same or lower than it.
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We're also able to compare this research output to 23 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 52% of its contemporaries.