Electron Crystallography
Electron Crystallography - Related Videos
02:18
X-ray Crystallography
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2020
The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography. Diffraction Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
09:23
Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
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Cited by 7 •
2010
Evaluating two-dimensional (2D) crystallization trials for the formation of ordered membrane protein arrays is a highly critical and difficult task in electron crystallography. Here we describe our approach in screening for and identifying 2D crystals of predominantly small membrane proteins in the range of 15 – 90kDa.
07:55
An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
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Cited by 4 •
2019
A novel sample holder for macromolecular X-ray crystallography along with a suitable handling protocol is presented. The system allows crystal growth, crystal soaking and in situ diffraction data collection at both, ambient and cryogenic temperature without the need of any crystal manipulation or mounting.
09:09
Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
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Cited by 20 •
2016
We describe procedures for the preparation and delivery of membrane protein microcrystals in lipidic cubic phase for serial crystallography at X-ray free-electron lasers and synchrotron sources. These protocols can also be applied for incorporation and delivery of soluble protein microcrystals, leading to substantially reduced sample consumption compared to liquid injection.
09:27
Protein Crystallization for X-ray Crystallography
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Cited by 71 •
2011
The 3-D structure of a molecule provides a unique understanding of how the molecule functions. The principal method for structure determination at near-atomic resolution is X-ray crystallography. Here, we demonstrate the current methods for obtaining three-dimensional crystals of any given macromolecule that are suitable for structure determination by X-ray crystallography.
FAQs
Electron crystallography can work with very small crystals because electrons interact strongly with matter. That interaction produces measurable diffraction information even when the ordered sample is smaller than the crystals typically required for X-ray crystallography. The practical consequence is access to structural targets that may be difficult to prepare in sufficiently large crystals for conventional X-ray analysis.
In two-dimensional protein arrays, electron microscope images provide projection views of regularly arranged molecules rather than relying only on a diffraction pattern. Combining these views computationally helps reconstruct molecular architecture, making the approach particularly informative for membrane proteins and other macromolecular assemblies whose organization is biologically important.
Computational reconstruction is central because individual diffraction patterns or microscope images do not directly provide a complete three-dimensional atomic model. Researchers combine the recorded information to infer molecular arrangement and compare structural states. This process can reveal conformational changes, meaning shifts in molecular shape or organization that may accompany biological activity.
Structural differences can connect a molecule’s architecture with its function. Reconstructed structures may be examined for features associated with ligand binding or for changes between conformational states. These observations help researchers investigate biological mechanisms and can provide structural evidence relevant to disease studies and drug-development efforts.
A typical workflow begins with a biological sample that forms a crystal or a regularly ordered array. An electron microscope then records either electron diffraction data or images of the ordered material. Computational analysis combines those measurements or projection views to reconstruct the three-dimensional arrangement, producing structural information that can be interpreted in a biological context.
The method is especially valuable when a target can be studied as a small crystal or as a two-dimensional protein array. Relevant examples include membrane-protein architecture and macromolecular complexes, as well as samples that adopt multiple conformational states. The resulting structures can clarify how molecular organization relates to biological function.
Electron crystallography supports disease and drug-development research by revealing structural features connected with ligand binding, molecular function, and conformational change. These observations can help relate a macromolecule’s three-dimensional organization to biological mechanisms. In turn, the structural information provides a basis for investigating disease-relevant changes and evaluating how molecular architecture may guide drug research.