We are proud of the progress made this year in developing and maintaining our research infrastructure facilities. We have seen new instruments acquired, installed and several are already hard at work providing research support to our University community. Some of these instruments provide new capabilities in throughput while others open brand-new areas of potential research inquiry. Utilization is greater this year in every facility, with some facilities reporting exponential jumps as new instrumentation comes on-line. The progress will not stop here, however. Already plans for new instrumentation, personnel and expertise development are underway. In the following paragraphs, the facility managers have outlined some of the highlights of their operations.

During the past year, the Laboratory for Biological Mass Spectrometry (LBMS) provided analysis on over 2,500 samples for over 45 research groups The LBMS also enjoyed many fruitful collaborative projects with researchers from the Chemistry Department as well as other departments and industry. A key addition to the lab is a PE-Sciex QSTAR Pulsar electrospray ionization TOF mass spectrometer housed in the laboratory of Professor David H. Russell. This instrument has a state-of-the-art hybrid LC/MS/MS Quadrupole TOF system capable of very high resolution (>10,000), high accuracy, and high sensitivity. The QSTAR can be equipped with either an ionspray and nanospray source, allowing for the analysis of microliter quantities of subpicomolar sample concentrations. The QSTAR is made available to LBMS users for both applications and collaborations. The 1999-2000 fiscal year also brought about some changes in staff. Jianhong Wang, Ph.D., was added in November, 1999, and has become a productive member of our staff. Kenneth Bullard left in August, 2000, and we are currently seeking his replacement.

The Crystal and Molecular Structure Laboratory reports that the new instrumentation, purchased in FY 1999-2000, has been fully utilized. Over 600 data sets have been collected on the three instruments and the current wait time is about two weeks. The laboratory has completed structures that were impossible to do in the past. We now routinely solve 500 to 700 atom structures. The record of a 768 non-hydrogen atom structure, a cyclododextrin, is one of the few such large structures to be solved by the Direct Methods structure solution technique. The laboratory was also awarded a major NSF grant totaling $530,000 for FY 2000-2001. The grant will be used to purchase three x-ray powder diffractometers. The new instrumentation will place the laboratory in the top three such facilities in the United States. The laboratory is concentrating on crystal structure solution from x-ray powder data. To this end our facilities will be the only such laboratory in the United States to offer its users this method on a full-time basis. An additional 600 square feet of laboratory space will be renovated to house the instrumentation. This will bring the total space of the facility to over 2000 square feet.

The Gene Technologies Laboratory provided DNA sequencing, oligo synthesis and reagent services to over 140 research groups from 6 TAMUS campuses, 6 colleges and over 25 departments. The demand for sequencing continues to escalate; the nearly 10 million bases (~ 23,000 reactions) sequenced in the past year represent a three-fold increase over the past four years with no increase in personnel.

This year has seen a change in the leadership of the Laboratory for Molecular Simulation with Lisa M. Thomson assuming the role as manager. During this transitional year, the laboratory has kept pace with an increasing demand for services and training. The heart of the laboratory is the server on which the molecular modeling software is installed, a SGI Power Challenge computer. This computer, with 12 processors, has been upgraded this year to some 1100 GB of disk storage space. The department=s Origin 2000 computer with four processors and 25 GB disk space is now on-line as well. Significant improvement and expansion of capabilities has also resulted from addition of software packages for both graphical visualization and chemical calculations. Additional workstations have been added to the server and important new application research is underway.

The Neutron Activation Analysis Laboratory has completed nearly 15,000 trace element determinations for university researchers--a record utilization. The effort focused on several large multielement studies in oceanography, animal science, entomology and anthropology; with most of the work performed by graduate students from those departments. The incorporation of two new gamma spectrometers and the installation of a new digital signal processor insures the laboratory has unsurpassed facilities. The unique fast neutron activation analysis capability has once again seen marked increases in demand. Services rendered to outside agencies has provided the funding for the upgrades this year and provided operational costs to help make the facility available for university use. We enjoyed collaboration with and support from fifty industrial and government customers.

During the past year, the NMR facility has logged nearly 33,000 hours on the nine NMR spectrometer systems in the facility. We provided access and service for over 300 separate users, and instructed nearly 70 new users on the systems. In July, Lana Frenkel left her position in the facility to move to Colorado with her family. That position is currently vacant and is in the process of being upgraded to a spectroscopist position and filled. A NSF proposal for the purchase of a walk-up, routine access 500 MHz spectrometer has been funded, and instruments are being evaluated to meet the growing need for routine access proton and carbon spectroscopy by the synthetic and natural products chemists.

Now in its third year of operation, the Protein Chemistry Laboratory has recently moved to larger laboratory space in the Biochemistry & Biophysics building and has added new personnel. Last year the laboratory initiated new programs in protein macro and micro-purification. The new Pharmacia Explorer 10 chromatographic system and an IPGPhor Isoelectric focusing unit purchased with extramural funds have been brought on-line and are being widely used by Texas A&M scientists. The versatile Explorer 10 is used to accelerate the development of protein purification protocols for new and novel proteins of biological interest as well as provide final stages of protein 'polishing' that are sometimes required by current microanalysis protocols. The IPGPhor system utilizes state-of-the-art immobilized pH gradient technology to perform 2-dimensional gel electrophoresis. It is used as an analytical tool to distinguish changes in profiles of cellular proteins and as a preparative tool to provide highly resolved micro-quantities of protein targets for further characterization including protein micro-sequencing and mass spectrometry. The laboratory=s schedule of workshops this year included, in addition to existing workshops on SDS PAGE and protein sequencing, several one-day lectures on liquid chromatographic techniques for protein purification and 2-dimensional gel electrophoresis techniques. This year the laboratory will add two new workshops: Theory and Practical Application of Reversed Phase HPLC and 2-D Gel Electrophoresis for Proteomic Analysis of Protein Mixtures. Additionally, the PCL staff have been involved in the development of a new inter-College Masters program in Biotechnology.

In addition to the seven labs described above, our report this year also contains an introduction to the new Biomolecular NMR Laboratory just formed during this last year. The new instruments associated with this new facility open the door for studying a wide array of large-molecule, biological interesting compounds for the first time.