Cryo Sem Crystal Structure
Cryo Sem Crystal Structure - Related Videos
18:45
Harvesting and Cryo-cooling Crystals of Membrane Proteins Grown in Lipidic Mesophases for Structure Determination by Macromolecular Crystallography
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Cited by 44 •
2012
Herein is described procedures implemented in the Caffrey Membrane Structural and Functional Biology Group to harvest and cryo-cool membrane protein crystals grown in lipidic cubic and sponge phases for use in structure determination using macromolecular X-ray crystallography.
02:42
Ionic Crystal Structures
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2020
Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size. Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...
22:00
Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
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Cited by 48 •
2010
Herein is described the procedure implemented in the Caffrey Membrane Structural and Functional Biology Group to set up manually crystallization trials of membrane proteins in lipidic mesophases.
11:27
A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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Cited by 2 •
2018
IκB Kinase 1/α (IKK1/α CHUK) is a Ser/Thr protein kinase that is involved in a myriad of cellular activities primarily through activation of NF-κB transcription factors. Here, we describe the main steps necessary for the production and crystal structure determination of this protein.
09:02
SEM Imaging of Biological Samples
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2023
Source: Peiman Shahbeigi-Roodposhti and Sina Shahbazmohamadi, Biomedical Engineering Department, University of Connecticut, Storrs, Connecticut A scanning electron microscope (SEM) is an instrument that uses an electron beam to nondestructively image and characterize conductive materials in a vacuum. As an analogy, an electron beam is to the SEM as light is to the optical microscope. The difference is that the electron microscope yields images of much higher resolution and magnification. The...
FAQs
Rapid freezing helps preserve hydrated biological or biomaterial specimens before drying can alter their architecture. Maintaining the frozen state allows researchers to examine crystal morphology, interfaces, and fine surface features in conditions closer to the original specimen. This is especially relevant when structural changes caused by dehydration would obscure relationships between crystal organization and biological function.
An electron beam scans the frozen specimen, and the emitted electrons are used to form an image of its surface architecture. Variations in the observed signal reveal differences in crystal morphology, interfaces, and fine structural detail. The resulting images provide spatial information about organization rather than the molecular-scale information obtained from complementary structural methods.
Cryo-SEM observations can be interpreted alongside information about composition and growth conditions to understand why crystals develop particular organizations. Their morphology and interfaces may also be considered in relation to biological function. This makes the technique useful for connecting visible structural patterns with the biological or material context in which the crystals formed.
The specimen is first rapidly frozen, then kept at cryogenic temperature while under vacuum. It is subsequently scanned with an electron beam, and the emitted electrons generate images for analysis. This workflow preserves features that may change during drying and enables examination of crystal surfaces, interfaces, and fine architecture in frozen biological or biomaterial samples.
Applications include biomolecular crystals, mineralized tissues, membranes, and other hydrated materials. These specimens can differ substantially in composition and organization, yet each may contain surface or interfacial features that are difficult to preserve after drying. Cryogenic imaging therefore supports comparative examination of crystal architecture across several biological and biomaterial settings.
Cryo-SEM contributes an architectural view by showing crystal organization, surface morphology, and interfaces in frozen specimens. Other structural methods can provide molecular-scale information, so combining the approaches connects larger-scale organization with finer structural detail. In biology, this comparison can help researchers interpret how crystal arrangement relates to composition, growth conditions, and function.