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Protein crystallization: from purified protein to diffraction-quality crystal
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Protein crystallization: from purified protein to diffraction-quality crystal
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Protein crystallization: from purified protein to diffraction-quality crystal
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Journal Article
Protein crystallization: from purified protein to diffraction-quality crystal
2008
Overview
Determining the structure of biological macromolecules by X-ray crystallography involves a series of steps: selection of the target molecule; cloning, expression, purification and crystallization; collection of diffraction data and determination of atomic positions. However, even when pure soluble protein is available, producing high-quality crystals remains a major bottleneck in structure determination. Here we present a guide for the non-expert to screen for appropriate crystallization conditions and optimize diffraction-quality crystal growth.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Biomedical and Life Sciences
/ Biomedical Engineering/Biotechnology
/ Chemistry, Physical - methods
/ Cloning
/ Crystals
/ Methods
/ Multiprotein Complexes - chemistry
/ Multiprotein Complexes - isolation & purification
/ Multiprotein Complexes - ultrastructure
/ Proteins
