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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Difficult Macromolecular Structures Determined Using X-ray Diffraction Techniques

Author(s): Alejandra Hernandez-Santoyo

Volume 19, Issue 7, 2012

Page: [770 - 777] Pages: 8

DOI: 10.2174/092986612800793181

Price: $65


Macromolecular crystallography has been, for the last few decades, the main source of structural information of biological macromolecular systems and it is one of the most powerful techniques for the analysis of enzyme mechanisms and macromolecular interactions at the atomic level. In addition, it is also an extremely powerful tool for drug design. Recent technological and methodological developments in macromolecular X-ray crystallography have allowed solving structures that until recently were considered difficult or even impossible, such as structures at atomic or subatomic resolution or large macromolecular complexes and assemblies at low resolution. These developments have also helped to solve the 3D-structure of macromolecules from twin crystals. Recently, this technique complemented with cryo-electron microscopy and neutron crystallography has provided the structure of large macromolecular machines with great precision allowing understanding of the mechanisms of their function.

Keywords: Atomic resolution, cryo-electron microscopy, crystallography software, low-resolution, macromolecular complexes, protein crystallography, twin crystal, X-ray crystallography, high-quality crystals, dynamic disorder

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