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Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....

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Updated: Mar 6, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Using more than 801 296 small-molecule crystal structures to aid in protein structure refinement and analysis.

Jason C Cole¹, Ilenia Giangreco¹, Colin R Groom¹

¹Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge CB2 1EZ, England.

Acta Crystallographica. Section D, Structural Biology

|March 15, 2017

Summary

This summary is machine-generated.

The Cambridge Structural Database (CSD) offers a vast collection of small-molecule structures. This resource aids macromolecular crystallography by validating protein-ligand complexes and generating restraints for structure refinement.

Keywords:

Cambridge Structural Database macromolecular crystallography scripting

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

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Last Updated: Mar 6, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Area of Science:

Crystallography
Structural Biology
Chemistry

Background:

The Cambridge Structural Database (CSD) is a comprehensive repository of published 3D structures for small-molecule organic and metal-organic compounds.
Macromolecular crystallography relies on accurate structural data for understanding biological processes.

Purpose of the Study:

To explore the utility of the Cambridge Structural Database (CSD) in the field of macromolecular crystallography.
To demonstrate how the CSD can enhance protein-ligand complex validation.
To illustrate the potential of the CSD in generating geometrical restraints for protein structure refinement.

Main Methods:

Utilizing the extensive collection of crystal structures within the CSD.
Applying associated software tools for data analysis and validation.
Investigating the generation of geometrical restraints from CSD data.

Main Results:

The CSD, when used en masse, provides valuable insights for macromolecular crystallography.
Examples demonstrate the effectiveness of CSD and software in validating protein-ligand complexes.
The CSD shows potential for generating crucial geometrical restraints in protein structure refinement.

Conclusions:

The Cambridge Structural Database is a powerful, versatile resource extending beyond small-molecule analysis.
Its application in macromolecular crystallography significantly aids in structure validation and refinement.
Further integration of CSD data can advance the accuracy and reliability of protein structural models.