Users are expected to keep the equipment and equipment areas safe, tidy, and very clean.
#Malvern zetasizer nano zsp laser direction full
The usage patterns of the SEC-MALS, Biacore T200, ProteomeLab XL-I, and MicroCal AutoiTC200 preclude hourly rates for these instruments the unit rates for these instruments are half day (4 hours) or full day (8 hours) of use. For usage totaling more than an hour, we charge for the actual time used. For instrument usage totaling less than an hour during a day, we charge for a full hour. Instruments are used (and billed) on an hourly or daily basis. We may bill no-shows and late cancellations, at our discretion. This is only fair to all who use the Facility. If you have made a reservation and wish to cancel it, please do so using CORUM as soon as you can. If the Facility is not notified or the reservation canceled, you may be billed for any time you reserve. Once you have reserved instrument time, please make every effort to be there and use it. You will be expected to make reservations and logon to instruments using your CORUM account. If you do not have an account, please log in here: to create one. The use of instruments or training, by the UMass-Amherst community, requires an advance reservation using CORUM. Training is provided by the core director. No one may gain access to the Facility using an ID not their own or use instruments for which they are not trained.Īll users must receive proper training before being permitted access to the Facility. Once trained, all registered users may request after-hours access. The Facility is staffed from 8:00AM until ~5PM on weekdays. Finally, we have a Rigaku x-ray source that will enable acquisition of small-angle x-ray scattering data as well as serving for single crystal diffraction, which we have already used for this project (preliminary data).įY21 Specialized Service Center Approved Fees In addition, our protein crystallography facility is equipped with a robotics crystallization set-up to prepare crystallization screens, along with the imaging stations necessary to monitor crystal growth. Rates are subject to change, contact facility to verify current fees.įY22 Specialized Service Center Approved Feesīiophysical Characterization Core Facility: MicroCal iTC-200 with auto-sampler, BiaCore surface plasmon resonance system, two Nanotemper thermophoresis instruments (one for proteins with extrinsic labels, the other for Trp excitation), a Biotek microplate reader equipped to detect absorbance, fluorescence, luminescence, and anistropy, an Odyssey Li-COR CLx imaging system, GE Typhoon phosphorimager, Beckman analytical ultracentrifuge with Aviv fluorescence detector, Malvern DLS/Zetasizer Nano ZSP system with MPT-2 (Titrator)/Degasser, Wyatt multi-angle light scattering instrument with Agilent chromatography system, and a JASCO M-1500 circular dichroism instrument.
Li-Cor Odyssey Imaging Microscale Thermophoresisīiotek Synergy 2 Plate Reader with Fluorosceneīeckman XL-I Analytical Ultracentrifuge with Aviv Fluorescence Detection structures, interactions, biological macromolecules, proteins, nucleic acids, lipids, complexes, virtual tour The instrumentation described below was chosen to enable the quantitative characterization of biological macromolecules and their interactions. The lab is also able to accept samples and perform the appropriate analysis for a quoted fee. We are able to offer our capabilities to researchers and invite them to use this equipment either on their own or with the help of faculty who have expertise in each method. The facility provides expertise and access to the latest, well-maintained instrumentation that is crucial to the research community of the University of Massachusetts system, the Five College system, other academic institutions, and industrial partners. This facility supports both discovery-based research and assay development for translational applications. Located on the 5th floor in the Life Science Laboratories the Biophysical Characterization facility houses 15 state-of-the-art instruments for the study of structures and interactions of biological macromolecules such as proteins, nucleic acids, lipids, and complexes.