منابع مشابه
Critical Review Electron Crystallography of Aquaporins
Aquaporins are a family of ubiquitous membrane proteins that form a pore for the permeation of water. Both electron and X-ray crystallography played major roles in determining the atomic structures of a number of aquaporins. This review focuses on electron crystallography, and its contribution to the field of aquaporin biology. We briefly discuss electron crystallography and the two-dimensional...
متن کاملElectron crystallography – an introduction
Everything in Nature, macroscopic or microscopic, inorganic, organic or biological, has its specific properties. Most properties of matter depend on the structures, and many techniques have been developed over the centuries for structure analysis. The greatest of them all, structure analysis of single crystals by X-ray diffraction, X-ray crystallography, was founded in 1912 and is still today t...
متن کاملElectron crystallography of membrane proteins.
Electron crystallography studies the structure of two-dimensional crystals of membrane proteins or other crystalline arrays. This method has been used to determine the atomic structures of six membrane proteins and tubulin, as well as several other structures at a slightly lower resolution, where secondary structure motifs could be identified. To preserve the high-resolution structure of 2D cry...
متن کاملSurface crystallography via electron microscopy.
The study of atomic structure of surfaces is fundamental to the understanding of electronic, chemical and mechanical properties of surfaces and numerous techniques have been developed to this end. Transmission Electron Microscopy techniques, namely transmission electron imaging (TEM) and diffraction (TED), due to their ability to provide structural information at very high resolutions, have eme...
متن کاملThree-dimensional electron crystallography of protein microcrystals
We demonstrate that it is feasible to determine high-resolution protein structures by electron crystallography of three-dimensional crystals in an electron cryo-microscope (CryoEM). Lysozyme microcrystals were frozen on an electron microscopy grid, and electron diffraction data collected to 1.7 Å resolution. We developed a data collection protocol to collect a full-tilt series in electron diffr...
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ژورنال
عنوان ژورنال: IUBMB Life
سال: 2008
ISSN: 1521-6543,1521-6551
DOI: 10.1002/iub.53