Macromolecular Structure Determination by X-ray Crystallography
Published Online: 3 MAY 2005
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Jaeger, J. 2005. Macromolecular Structure Determination by X-ray Crystallography. eLS. .
- Published Online: 3 MAY 2005
This is not the most recent version of the article. View current version (15 JUL 2014)
X-ray diffraction is a well-established method to elucidate the atomic structure of single-crystal macromolecules. An image of the macromolecule forming the crystal cannot be directly recorded as the X-ray phase information is lost during the diffraction experiment. Through systematic variation of the chemical content in the crystal and/or through small changes in the wavelength of the incident X-ray beam, however, a sharp image can be reconstituted computationally. Within the Protein Data Bank, the vast majority of three-dimensional structures available have been determined using X-ray diffraction. These structures are used to correlate macromolecular structure with function, to study molecular mechanisms and serve as templates for structure-based drug design of novel therapeutic agents for the treatment of many diseases.
- atomic structure;
- phase problem;