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Searching for silver bullets: an alternative strategy for crystallizing macromolecules.

Alexander McPherson¹, Bob Cudney

¹University of California, Irvine, Department of Molecular Biology and Biochemistry, Room 560 Steinhaus Hall, Irvine, CA 92697-3900, USA. amcphers@uci.edu

Journal of Structural Biology

|November 15, 2006

Summary

Small molecules can improve protein crystallization by forming non-covalent crosslinks. This study screened 200 chemicals, finding many enhance protein and virus crystallization, suggesting a new approach for structural biology.

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Area of Science:

Structural Biology
Biochemistry
Crystallography

Background:

Protein crystallization is crucial for determining protein structures.
Identifying effective crystallization conditions remains a challenge.
Small molecules may stabilize protein crystals through non-covalent interactions.

Purpose of the Study:

To investigate the impact of small molecules on protein and virus crystallization.
To identify chemical additives that promote lattice formation.
To develop an alternative strategy for protein crystallization.

Main Methods:

Screening 200 chemicals across 81 proteins and viruses.
Conducting 18,240 vapor diffusion trials.
Utilizing two fundamental crystallization conditions (30% PEG 3350, 50% Tacsimate at pH 7) with additive mixes.

Main Results:

65 out of 81 proteins (85%) were successfully crystallized.
35 proteins (54%) crystallized only with the addition of small molecule mixes.
Promising additives included polyvalent charged groups, biochemicals, coenzymes, and ligands.

Conclusions:

Small molecule additives significantly enhance protein crystallization success rates.
A combination of limited basic conditions and diverse small molecule screening is effective.
This approach offers a novel strategy for protein structure determination.