Crystal Harvesting
Crystal Harvesting - Related Videos
18:45
Harvesting and Cryo-cooling Crystals of Membrane Proteins Grown in Lipidic Mesophases for Structure Determination by Macromolecular Crystallography
0 Views •
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.
07:39
Protein Crystallization
0 Views •
2023
Protein crystallization, obtaining a solid lattice of biomolecules, elucidates protein structure and enables the study of protein function. Crystallization involves drying purified protein under a combination of many factors, including pH, temperature, ionic strength, and protein concentration. Once crystals are obtained, the protein structure can be elucidated by x-ray diffraction and computation of an electron density model. This video introduces protein crystallization and shows a general...
13:38
Synthesis of Biocompatible Liquid Crystal Elastomer Foams as Cell Scaffolds for 3D Spatial Cell Cultures
0 Views •
Cited by 9 •
2017
This study presents a methodology to prepare 3D, biodegradable, foam-like cell scaffolds based on biocompatible side-chain liquid crystal elastomers (LCEs). Confocal microscopy experiments show that foam-like LCEs allow for cell attachment, proliferation, and the spontaneous alignment of C2C12s myoblasts.
11:53
Crystallization of Membrane Proteins in Lipidic Mesophases
0 Views •
Cited by 30 •
2011
The protocols describe the essential steps for obtaining diffraction quality crystals of a membrane protein starting from reconstitution of the protein in a lipidic cubic phase (LCP), finding initial conditions with LCP-FRAP pre-crystallization assays, setting up LCP crystallization trials and harvesting crystals.
09:35
Microcrystallography of Protein Crystals and In Cellulo Diffraction
0 Views •
Cited by 9 •
2017
A protocol is presented for X-ray crystallography using protein microcrystals. Two examples analyzing in vivo-grown microcrystals after purification or in cellulo are compared.
FAQs
Isolation from the mother liquor gives the researcher access to an individual crystal that can be handled with a fine loop or comparable tool. The crystal can then be transferred, when necessary, into cryoprotectant and rapidly cooled. These actions connect physical recovery with preservation of the crystal lattice, allowing the specimen to proceed to structural analysis.
Rapid cooling helps preserve the crystal lattice during handling and prepares the specimen for downstream structural analysis. Because harvesting moves the crystal away from its original crystallization condition, cooling provides a preservation step when cryoprotection is required. The outcome is a crystal retained in a state suitable for subsequent X-ray crystallographic examination.
A fine loop provides a means to isolate and manipulate an individual crystal without relying on bulk recovery from the crystallization experiment. Its use supports controlled transfer from the mother liquor to cryoprotectant when needed, followed by rapid cooling. Careful manipulation is therefore central to maintaining the specimen for structural analysis.
The workflow begins by selecting an individual crystal from the crystallization experiment and retrieving it from the mother liquor with a fine loop or similar tool. When required, the crystal is transferred into cryoprotectant and then rapidly cooled. The harvested specimen can subsequently support X-ray crystallography and three-dimensional structural determination.
Cryoprotectant is used when the harvested crystal requires additional protection before rapid cooling. The material is introduced during transfer from the mother liquor, creating a preservation step between isolation and cooling. Its use is part of a conditional workflow rather than an automatic requirement, so harvesting procedures can be adapted to the needs of the crystal.
Harvested crystals support X-ray crystallography, which can determine three-dimensional structures of proteins, nucleic acids, and molecular complexes. These structures provide a basis for examining function, interactions with ligands, and roles in catalysis, signaling, or drug recognition. In this way, careful sample recovery connects a crystallization experiment with mechanistic questions in biology.