Abstract
The elucidation of the three dimensional structure of biological macromolecules has provided an important contribution to our current understanding of many basic mechanisms involved in life processes. This enormous impact largely results from the ability of X-ray crystallography to provide accurate structural details at atomic resolution that are a prerequisite for a deeper insight on the way in which bio-macromolecules interact with each other to build up supramolecular nano-machines capable of performing specialized biological functions. With the advent of high-energy synchrotron sources and the development of sophisticated software to solve X-ray and neutron crystal structures of large molecules, the crystallization step has become even more the bottleneck of a successful structure determination. This review introduces the general aspects of protein crystallization, summarizes conventional and innovative crystallization methods and focuses on the new strategies utilized to improve the success rate of experiments and increase crystal diffraction quality.
Highlights
Genome-sequencing projects have provided a near complete list of the molecules that are present or potentially present in an organism, and post-genomic projects are aimed at cataloguing theInt
This paragraph is a brief summary of the conventional methods that are commonly employed in the crystallization of macromolecules: vapor diffusion, free interface diffusion (FID), batch and dialysis
The results indicate that reducing the initial concentration of the crystallization agent in the droplet leaving the protein concentration unchanged increases the rate of vapor diffusion and produces higher success rate of protein crystallization
Summary
Genome-sequencing projects have provided a near complete list of the molecules that are present or potentially present in an organism, and post-genomic projects are aimed at cataloguing the. Depending on the level of supersaturation this zone of the diagram can be divided into three regions: very high supersaturation (“precipitation”), where molecules form amorphous aggregates [13], intermediate supersaturation (“labile”), where both growth and nucleation occur, and lower supersaturation (“metastable”), where only growth is supported. The present work will review some of the basic ideas and principles of biological macromolecule crystallization, summarize the standard approaches in crystal growth and illustrate novel tools and strategies to increase the rate of positive results and the diffraction quality of crystals This manuscript focuses mainly on soluble proteins, but covers the crystallization of membrane proteins, nucleic acids and nucleic acids/protein complexes, and discusses general physico-chemical aspects of the crystallization mechanisms
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