Cryo Electron Microscopy
CWRU cryo-Electron Microscopy (Cryo-EM) facility houses state-of-the-art electron microscopes in a newly renovated space including FEI Titan Krios G3i 300 kV X-FEG TEM with BioQuantum K3, Phase Plate; an FEI Tecnai TF20 (200kV, FEG) transmission electron microscope with a 4k x 4k CMOS-based Tietz TemCam-F416 and a DE-20 direct electron detector, and FEI Tecnai G² Spirit (120kV) transmission electron microscope with a 4k x 4k Gatan US4000 CCD camera; The facility is set up to prepare flash-frozen samples for single particle, cryo- electron tomography, and crystallography analysis.
The Facility also offers complete conventional TEM services including sample processing, ultramicrotomy, film developing, and photographic printing, as well as immunocytochemistry.
Intramural collaboration is available. We welcome trained EM users as well as researchers who wish to be trained.
Nuclear Magnetic Resonance
Nuclear Magnetic Resonance (NMR) Spectroscopy is a very versatile technology for the characterization of structure and dynamics of small molecules as well as biological macromolecules in solution (even as part of mixtures and in cells), but also in membrane mimicking environments, in solid powders or microcrystals. The facility houses state of the art equipment primarily for solution NMR (Bruker 600, 700, 800 and 900 MHz spectrometers), and a solid state capacity has been added to the Bruker 800 MHz spectrometer. Recently we were able to update the 600 and 700 MHz spectrometers to HDneo consoles and install new cryoprobes with superior sensitivity and capability to do direct 13C detect as well as 19F experiments.
Proteomics and Small Molecule Mass Spectrometry Core
CWRU Proteomics Core in collaboration with the Case Center for Proteomics and Bioinformatics (CPB) was established in 2006. Now called Proteomics and Small Molecule Mass Spectrometry the core provides state-of-the-art proteomic instrumentation, computational resources and software for systems biology, proteomic methods development, consultation, and training. The proteomics core is highly experienced in both structural and quantitative proteomics and core staff actively collaborates in grant proposals and development of novel technologies that applies proteomics/mass spectrometry to biomedical research. Areas of expertise include the development novel LCMSMS assays, unbiased shotgun quantitative proteomic analyses (label free protein expression and ITRAQ), global phosphoproteomics, post-translation modification analysis, X-ray footprinting MS, and general mass spectrometry services.
Synchrotron X-Ray Footprinting
Synchrotron X-ray footprinting provides a method of observing the structure and dynamics of biological macromolecules and their interactions in the solution state (in some cases within living cells) at the single nucleotide or single amino acid level. This method is unique in providing "local" structural information in solution for gaining insight into dynamic processes involving large RNA-protein and protein-protein assemblies at a higher resolution on biologically relevant timescales and under physiological conditions. Synchrotron-based footprinting studies have provided novel insights and approaches for steady state and time-resolved studies of macromolecular dynamics, examining the structure of large macromolecular assemblies, in vivo studies of macromolecules, and even observing functional water dynamics within the context of these biological structures. The XFP beamline at NSLS-II, developed and operated by the CSB in partnership with NSLS-II, is the premier facility in the world dedicated to synchrotron footprinting studies.
Protein Expression and Purification crystallization Core
PEPCC is a state-of-art laboratory that provides access to protein expression purification crystallization and molecular biophysical instrumentation. The PEPCC operates as an open, shared-used facility and provides training, technical expertise and assistance to all users. PEPCC provides services in protein expression and purification, automated crystallization, biophysics, and imaging.