Research Facilities
There is an impressive array of facilities and research instrumentation available for participants in the Microbial Biology program at the University of Utah.  Facilities are available within Biology for routine physical measurements needed to support various research efforts. In addition, the other departments at the University of Utah emphasize particular research areas and have the sophisticated instrumentation to support these activities.  The major instruments (NMR, mass spectrometry, FT-IR, ESR, X-Ray diffraction, supercomputer) are available to users campus-wide, and interdepartmental collaborations involving these instruments are encouraged.  There are instruments available for UV-Vis, IR, CD, titration-calorimetry, analytical ultra-centrifugation, and polarimetry.  Groups in the Chemistry department are using scanning tunneling microscopy and atomic force microscopy to study the structure of biological macro-molecules.  For projects involving large-scale structures, confocal microscopes are located in the Imaging Core Facility.  The Microbial Biology program also has state-of-the-art deconvolution fluorescent microscopes available for protein localization studies in bacteria.

Biomolecular NMR Facility
Jack Skalicky, Ph.D., Director
The Biomolecular NMR Core Facility exists to facilitate the determination of new protein, nucleic acid, and natural product structures and to provide analytical NMR services to the Health Sciences community.  The facility provides the necessary hardware and software for NMR data acquisition and analysis; it also has a centralized computing facility and detailed protocols for the various steps involved in biomolecular NMR structure determination.  NMR instrumentation includes a Varian Unity 500 MHz NMR spectrometer, a Varian Inova 600 MHz NMR spectrometer and a Varian Mercury 400.  The NMR center also has several Sun and SGI workstations for offline data processing and biomolecular structure determination.  Instrument schedules, rates, detailed instructions for using the facility, and instrument request forms are available on the website.

High Performance Computational Resources
Julio Facelli, Ph.D., CHPC Director
In addition to dedicated computational resources for biological chemistry research programs available in specific labs and departments, the Center for High Performance Computing (CHPC) provides training, software, and access to high performance computational resources for the larger campus community.  Currently available hardware resources include an 8-node (32 processor)) Compaq Sierra cluster with a QUADRIX switch and the Icebox cluster of ~303 nodes (388 processors) of Intel and AMD processors.  Additional specialized servers are available for specific applications like large-scale statistics, molecular modeling, Genbank searches, etc.  During the summer of 2003, a large NIH and University of Utah funded metacluster for bioinformatics ($2,000,000) came online.  This includes  a series of interconnected cluster computer including a high performance parallel cluster, a data mining cluster, a visualization capabilities including an AccessGrid node (allowing realtime video conferences to other AccessGrid nodes throughout the world) and training.  For more information, see http://www.chpc.utah.edu.

DNA and Peptide Facility
Bob Schackmann, Ph.D., Director
This core offers investigators synthetic peptides for use in generating antibodies; and it also provides oligonucleotide synthesis services for use as primers in PCR experiments, hybridization studies, and for DNA sequencing.   This core also offers Edman protein/peptide sequencing.

Electron Microscopy Facility
Kurt Albertine, Ph.D., Director, kurt.albertine@hsc.utah.edu
This facility provides a variety of microscopy services to the basic science and clinical communities.  Services and technical capabilities include light microscopy (brightfield, fluorescence, 3-D, etc.), trans-mission and scanning electron microscopy (quantitative morphology), histochemistry, immunohistochemistry,in situ hybridization, laser capture microscopy, PCR, RT-PCR and in situ PCR/RT.PCR.

Mass Spectometry and Proteomics Facility
Chad Nelson, Ph.D., Director
This core provides mass spectrometry services and consultation to laboratories and other research groups.  These measurements are utilized in a range of investigations involving molecular characterization, such as identification of mutanegized proteins from 1D or 2D gels, or characterization of potential anti-tumor agents.  Molecular mass measurements are made with typical errors of +/- 2Da at Mr 25kDa.  Partial sequencing of small peptides can be carried out, at the 300 femtomole and higher level, in peptide mixtures or tryptic digests of proteins.  Protein identification services include protein database searching using Sequest or Mascot software.  Data are acquired using electrospray ionization LC/MS/MS techniques, or by matrix-assisted laser desorption ionization (MALDI) time-of-flight (TOF) mass spectrometry.

Protein Interaction Facility
David Myszka, Ph.D., Director
The Protein Interaction Facility provides easy access to advanced technologies used in characterizing binding interactions.  Currently BIACORE 3000, 2000 and S51 optical biosensors are used to define the assembly state, affinity, and kinetics of an interaction.  The advantage of optical biosensors is that they allow real-time analysis of molecular interactions without labeling requirements.  This makes the technology applicable to the study of a wide variety of biological molecules including proteins, oligonucleotides, oligosaccharides and lipids.

Genomics Facility
Helaman Escobar, Director
The Genomics Facility provides a cost effective, high throughput genotyping and fragment analysis service to the University community. The facility utilized fluorescent PCR technology and state-of-the-art capillary instrumentation to collect and analyze genotypes from human and mouse DNA samples.  Technical services include genome scans, fine mapping, microsatellite instability (replication error), allelic imbalance (loss of heterozygosity) and single nucleotide polymorphism detection.  The facility will also soon introduce instrumentation for high throughput real-time quantitative PCR and SNP genotyping.

X-ray Crystallography
The department of Biology is involved in structure determination using X-ray sources and computer interfaced detectors are used to obtain the high-quality diffraction data required to determine protein structures at high resolution. As described above, a large amount of computer resources are devoted to crystallographic refinement and to analyzing protein structures using molecular graphics systems.