The Department of Biochemistry has excellent facilities for X-ray diffraction analysis of proteins and nucleic acids. The X-ray faciliies occupy most of the second, third, sixth floor of the 1985 wing of the department’s complex, and provide more than 10,000 square feet of laboratory and office space. Complete remodeling and renovation of the second and third floor for crystallography is scheduled to be completed by May 2001. This will provide two temperature controlled crystallization rooms, an 800 sq. ft. and 170 sq. ft. coldroom, and ample lab space for crystal manipulation and growth. There is sufficient space to store over 20,000 crystallization plates. The sixth floor is being optimized for computational studies, but also has excellent space for protein purification and crystal growth. An additional 170 sq. ft. cold room is available for structural studies. It is anticipated that considerably more space will be available once the structural biology addition is completed in 2007 (see below).

The X-ray diffraction laboratory contains two Rikagu RU200 generators equipped and will contain four area detectors. These consist of three Bruker Hi-Star detectors and an RAXIS-IV++ detector that is on order. Three of the detectors are equipped with cryogenic cooling; all have data collection abilities for 4°C. There is also a remote cryogenic station for optimizing crystallization conditions prior to examination with X-rays. The RAXIS-IV++ detector will be equipped with confocal optics for maximum flux, whereas the Hi-Star detectors utilize Goebel mirrors and Supper Long-mirrors to provide a well focused X-ray beam.

The computational environment is also state-of-the-art. Every office desk will include two network connections. Graphics workstations, compute clusters, and file servers are available as needed. A virtual reality system is also under development for modeling, crystallography, and molecular dynamics work. This system, based on the ImmersaDesk by Fakespace, allows glove-activated ‘hands-on’ work on biomolecules.

UW-Madison is also less than three hours by car to the Advanced Photon Source (APS) at Argonne National Laboratory , the most powerful synchrotron facility in the United States. The APS has multiple beamlines for macromolecular crystallography, and is regularly used by UW crystallographers.

National Magnetic Resonance Facility at Madison (NMRFAM)

The Biochemistry Department houses the National Magnetic Resonance Facility at Madison (NMRFAM), a shared instrumentation facility supported by a grant from the Biomedical Technology program of the NIH National Center for Research Resources. NMRFAM contains five modern multinuclear NMR spectrometers (currently all Bruker). These operate at field strengths (¹H frequencies) of 9.4 Tesla (400 MHz), 11.74 Tesla (500MHz) [two spectrometer systems, one with a high-sensitivity cryogenic triple-resonance probe and one with conventional probes], 14.1 Tesla (600 MHz), and 17.63 Tesla (750 MHz). Also available at NMRFAM are a computer server and a network of computer workstations with access to a wide range of software packages relevant to NMR spectroscopy and structural biology. A team of 12 staff members (10 with Ph.D. degrees) carry out core research and development projects on their own and as collaborations and make a wide range of technology available to users of the facility. Funded core projects focus on (1) software development for high-throughput structure determination, (2) NMR approaches for obtaining novel information about hydrogen bonding in proteins and nucleic acids, (3) use of computational chemical approaches to determineNMR observables, (4) improved methods for producing stable-isotope-labeled proteins for NMR investigations, and (5) low-viscosity approaches to NMR line narrowing for investigations of larger biomolecules. In the coming months, NMRFAM plans to place orders for new spectrometers operating at 14.1 Tesla (600 MHz), 18.8 Tesla (800 MHz) and 21.1 Tesla (900 MHz).

BioMagResBank (BMRB)

BioMagResBank (BMRB) is the publicly-accessible depository for NMR results from peptides, proteins, and nucleic acids recognized by the International Society of Magnetic Resonance and by the IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. In addition, BMRB provides reference information and maintains a collection of NMR pulse sequences and computer software for biomolecular NMR. Access to data in BMRB is free directly from its web site (URL http://www.bmrb.wisc.edu) and ftp site (ftp.bmrb.wisc.edu).