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Facilities
Genomics Core Facility
The genomics core facility, located in the Bioscience Research Building room 2229, enables researchers to conduct high throughput DNA sequencing and gene expression analyses enhanced by the use of robotics. This allows researchers to obtain important information about the genomes of bacteria, parasites, fish or other organisms in a much shorter time than was previously possible. Contact Dr. Tom Kocher or Dr. Najib El-Sayed for details.
Proteomics Core Facility
The proteomics core facility, located in the Bioscience Research Building room 2219, features a Thermo Finnigan LTQ Orbitrap tandem mass spectrometer, interfaced with an Accela Ultra High Pressure Liquid Chromatography, which is acquired through a multi-user NIH-grant organized by Catherine Fenselau, professor of chemistry and biochemistry, and supported by the college. This technology allows researchers to identify and map individual proteins in complex biological samples, such as blood, serum, or even bacteria, and to determine their function. Director: Dr. Yan Wang: yanwang@umd.edu, Office: 5-6764, Lab: 5-8425
Flow Cytometry and Cell Sorting Facility
The flow cytometry core facility, located in the Bioscience Research Building room 2102, includes a BD Biosciences FACSAria II Cell Sorter, jointly funded by a multi-user NIH-grant authored by David Mosser, professor and director of the Maryland Pathogen Research Instititute (MPRI) and funds from the College. This sophisticated machine provides a method for sorting a heterogeneous mixture of cells, one cell at a time, based upon specific characteristics of each cell, and collecting them as homogenous populations for analysis. Director: Ken Class, kclass@umd.edu, Office: 54593, Lab: 50398
Imaging Core Facility
The Imaging Core provides faculty and students the opportunity to image live, fixed, unlabeled or fluorescently labeled samples using one of several available microscopes.
Nuclear Magnetic Resonance (NMR) Spectroscopy
This facility, located in room B0130 of the Chemistry Building, is equipped with five Bruker NMR spectrometers, and twenty different NMR probes to meet various research demands and applications. In 2008, the department added two new 600 MHz nuclear magnetic resonance (NMR) spectrometers, funded by a multi-user grant from the National Science Foundation. One of these spectrometers, combined with pre-existing instrumentation, is now the core facility for a group of experts in biomolecular NMR spectroscopy including David Fushman, Professor; Vitali Tugarinov, Assistant Professor; and Kwaku Dayie, Associate Professor; who all study the intricate structure and dynamics of proteins and nucleic acids. The second 600 MHz NMR spectrometer has enabled advances in materials science, including the technology developed by Lawrence Sita, professor of chemistry and biochemistry, that can produce a wide variety of plastic products which are safe for the environment and human health.
Mass Spectrometry
The Mass Spectrometry Facility is equipped with several high-performance mass spectrometers to support basic research efforts throughout the University of Maryland. The facility is located in room 1515 of Building 091, Department of Chemistry & Biochemistry. The facility offers training for independent operation of instruments as well as sample analysis by facility personnel. The facility’s services are also open to external academic institutions and industry.
X-ray Crystallography
X-ray Photoelectron Spectroscopy
This facility, located in the Chemistry Building, contains a high sensitivity Kratos AXIS 165 spectrometer which is used to to obtain the structures of complex molecules. The analysis is done by irradiating a sample with soft x-rays to ionize atoms and releasing core-level photoelectrons. The kinetic energy of the escaping photoelectrons limits the depth from which it can emerge, giving XPS its high surface sensitivity and sampling depth of a few nanometers. Photoelectrons are collected and analyzed by the instrument to produce a spectrum of emission intensity versus electron binding energy.






