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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Updated: May 24, 2026

High-Throughput Protein Crystallization via Microdialysis

High-Throughput Protein Crystallization via Microdialysis

Published on: March 3, 2023

Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization.

Monica Totir¹, Nathaniel Echols, Max Nanao

¹Department of Molecular and Cell Biology, University of California, Berkeley, California, United States of America.

|March 7, 2012

Summary

This summary is machine-generated.

This study explored using native source proteins from Escherichia coli for high-throughput protein crystallography. Researchers successfully determined 23 protein structures, demonstrating a viable alternative to recombinant expression for structural biology.

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High-Throughput Protein Crystallization via Microdialysis

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Protein Crystallization for X-ray Crystallography

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Area of Science:

Structural Biology
Structural Genomics
Biochemistry

Background:

Recombinant protein expression is standard for structural biology but often challenging for many proteins and complexes.
Difficulties in obtaining proteins via recombinant methods limit structural studies.

Purpose of the Study:

To investigate the utility of native source proteins for high-throughput protein crystallography.
To establish a method for obtaining protein structures from native sources.

Main Methods:

Fractionation and purification of the Escherichia coli proteome.
Crystallization of protein fractions using microfluidic chips.
Structure determination through X-ray diffraction analysis.

Main Results:

408 unique soluble proteome fractions were generated.
295 fractions yielded crystals, with 152 selected for further analysis.
23 protein structures were determined, including 4 novel structures.

Conclusions:

Native source proteins are a practical alternative for high-throughput crystallography.
This approach expands the scope of proteins amenable to structural determination.
The study validates a novel strategy for structural genomics projects.