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Macromolecular Structure Determination by X-ray Crystallography

  1. Joachim Jaeger

Published Online: 3 MAY 2005

DOI: 10.1038/npg.els.0002723



How to Cite

Jaeger, J. 2005. Macromolecular Structure Determination by X-ray Crystallography. eLS. .

Author Information

  1. Wadsworth Center, Albany, New York, USA

Publication History

  1. 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.


  • diffraction;
  • atomic structure;
  • phase problem;
  • crystallization