What is the mission of the UCLA DOE Institute?
The mission of the UCLA-DOE Institute Crystallography and Structure Determination Core is to provide state-of-the-art resources to researchers at UCLA., enabling the detailed 3-D analysis of biological macromolecules that play essential roles in human health. The facility operates as a full service core that not only offers access to sophisticated equipment and technologies, but also offers advice and technical assitance in sample preparation, data collection, processing, atomic refinement and modeling.
What is the cold room in X-ray?
The cold room also is equipped for crystal growth and mounting of heat-labile crystals. The compressors and water recirculating coolers used to remove heat from the x-ray generators are kept in the small room 116, to isolate the noise from the rest of the facility.
What microscopes are used in IGP?
The facility incorporate emerging technologies, adding new instruments now available to IGP investigators: 1) The 300Kv Tecnai F30, 2) The 120kV Tecnai T12 TEM microscope, 3) An Acoustic Liquid Handling ( Echo Labcyte) for crystallization, synthetic biology and functional screening. 4) An Octet RED96 (ForteBIO) to measure kinetics and ligand binding. 5) A Wyatt DynaPro Plate Reader to measure Dynamic and Static Light Scattering. Also we have regular access to a new 200kV Talos instrument that will further bolster capabilities in MicroED, CryoEM and tomography.
What is X-ray structure determination?
The X-ray and EM Structure Determination Core conducts original research in improving crystallographic tools, continuously developing data collection techniques and processing pipelines (indexing, integration, scaling) and have added electron microscopy methods to our existing X-ray capabilities. Each structure determined using the core facility not only yields biological insights, but also expands databases used in algorithms for fold assignment, structure verification, atomic refinement, potential energy functions, and analysis of protein-protein interactions. Comprehensive databases are key to maintaining and improving these vital tools that enable reliable, high quality structure determination and prediction.
What is the purpose of UV/VIS microscope?
UV/vis microscope to determine whether crystals are composed of protein or salt.
What is the purpose of protein crystallography?
Racemic protein crystallography refers to the idea of crystallizing proteins from a racemic mixture of the natural, biologically-handed, molecule and its mirror image molecule (reviewed in Yeates and Kent, 2012). The latter must be chemically synthesized in the laboratory from D-amino acids while the natural molecule may be synthezised or expressed in a biological host by using traiditional molecular biology methods. Laura Zawadzke and Jeremy Berg were the first to execute the idea in 1993 using the small (45 amino acid) protein rubredoxin. An early motivation for pursuing such studies was the idea that structure determination might be easier or more robust using diffraction data from a centrosymmetric crystal, which requires growth from a racemic mixture. There are merits to this idea, and recent work has further explored the possibilities of certain advantages in phasing centrosymmetric protein diffraction data (Sawaya et al., 2012).
When was ligation first used?
The invention of native chemical ligation methods by Phil Dawson and Stephen Kent in the early 1990’s opened up prospects for chemically synthesizing larger protein molecules. Kent and co-workers have since tested racemic crystallography on a wide range of protein molecules. Current data provide strong support for the idea that proteins do crystalize with realtive ease from synthetic racemic mixtures (and most often in P1 (bar) as predicted).
THE MicroED CORE
The MicroED Core is a cryo-EM facility based at UCLA’s David Geffen School of Medicine, dedicated to make MicroED structure solution accessible to academia and industry. Services include all steps from sample mounting to refined structure, according to your needs and in order to suite your workflow.
SERVICES
Services include all steps toward a refined structure as needed, including sample mounting, initial screening and diffraction analysis, data collection, structure solution, and model refinement. Any additional work can be performed as requested on an hourly payment basis.
GET IN TOUCH
We are happy to answer any questions regarding our services, explain how we fit into your project, or provide any further information you may need to try MicroED.
Short Biography
David Eisenberg is a Professor of Chemistry and Biochemistry and of Biological Chemistry at the University of California, Los Angeles, and Director of the UCLA-DOE Institute for Genomics and Proteomics. He received his undergraduate degree in biochemical sciences from Harvard College and his D.Phil.
Biography
David Eisenberg is currently Professor of Chemistry and Biochemistry and Biological Chemistry, as well as HHMI Investigator and Director of the UCLA-DOE Institute for Genomics and Proteomics. Before he came to UCLA, Eisenberg earned an A.B. in Biochemical Sciences from Harvard College and a D.Phil.
Research Interests
David Eisenberg and his research group focus on protein interactions. In their experiments they study the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state.