History and future of X-ray structure determination
Part 3. Proteomics
3.7. Structural Proteomics
Published Online: 15 JUL 2005
Copyright © 2005 John Wiley & Sons, Ltd
Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics
How to Cite
Jaeger, J. and Dennis, C. 2005. History and future of X-ray structure determination. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.7:95.
- Published Online: 15 JUL 2005
Single crystal X-ray diffraction was first applied at the beginning of the twentieth century and to this day remains the most commonly used and highly productive technique to elucidate macromolecular structures at the atomic level. Recent developments in the theoretical background and in computational methods, dramatic improvements in experimental designs of synchrotron beamlines and insertion devices, and technical advances in high-throughput methods combined with robotics have had a major impact on the analysis of macromolecular structure. Combination of cryogenic imaging techniques (EM) with multidimensional NMR, X-ray, and electron diffraction studies will lead to unprecedented, new insights into the structure–function relationships of biological macromolecules.
- macromolecular structure;
- X-ray crystallography;
- phasing methods;
- synchrotron radiation