Biomolecular Crystallography Facility
The Biomolecular Crystallography Facility provides exceptional in-house X-ray diffraction capabilities using a Bruker D8 Venture system. The D8 Venture is equipped with an extreme brightness Excillum D2+ MetalJet X-ray source employing a liquid gallium alloy jet anode capable of accepting significantly higher power loads than conventional solid metal targets. The liquid gallium anode allows for extremely small electron spot sizes provided using a LaB6 cathode and an electronically controlled focusing coil. A HELIOS MX optic focuses the X-ray beam with multiple options to control beam divergence according to crystal size and unit cell parameters. Crystals mounted on the kappa-axis goniometer can be presented to the beam in any orientation to provide complete coverage of the reciprocal lattice. A PHOTON II charge-integrating pixel array detector allows for low noise, shutterless data collection. Crystals are mainained at cryogenic temperatures with an Oxford Cryosystems Cryostream 800 cryostat. Data collection and processing is managed using Bruker Proteum3 software for macromolecular crystals and with Bruker Apex3 software for small molecule crystals.
The facility exists to make structural analysis by crystallography available to researchers on the Vanderbilt campus by providing state-of-the-art equipment and instrumentation, training, software, and support for all aspects of crystal structure solution. We strive to help crystallographers accomplish their work efficiently while being able to push the boundaries of the technology. The facility is also available to train and support researchers wanting to learn crystallography as a valuable research tool.
Pac@Van: Protein Automated Crystallography @ Vanderbilt
The Vanderbilt Center for Structural Biology includes a high-throughput crystallization facility with four integrated components: 1) a Hamilton Star-Let liquid handler; 2) a Mosquito nano-liter drop setter; 3) a Xantus Cubic Lipid handling robot; and 4) a Formulatrix imager with UV fluorescence detector. These robots are located on the 4th floor of the Robinson Research Building in a 400 ft2 temperature-controlled room, currently maintained at 20°C. Bar-coding coordinates the information transfer between robotic instruments, which can be operated remotely through the network. The automated crystallization facility has improved the efficiency of making crystallization screens, increased the speed of initial crystallization trials, decreased the amount of sample need for crystallization, decreased the amount of time required to analyze the crystals, and decreased the rate of false positives. Training on the instruments maintained within the robotic facility is available through individual consultations.
View the current schedule, and contact Joel Harp for access.
Crystallography allows for direct visualization of molecular structure at the atomic level. X-ray crystallography is the primary tool for the structural analysis of proteins and nucleic acids accounting for 85% of all models in the PDB. Macromolecular structures determined by X-ray crystallography provide answers to questions relating to molecular structure including issues of domain and fold architecture, ligand recognition and binding, and details of atomic bonding.
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