The center piece of the Protein X-Ray Crystallography Facility is a Rigaku HighFlux HomeLab system made possible through a past award from the Vice Provost for Research. This Facility is housed in the basement of the Pharmacy/Biology Building, Room 054 and is available to the University of Connecticut research community including postdoctoral fellows and students as well as academic and industrial laboratories across the northeast. Drs. Amy Anderson and Victoria Robinson, both experts in protein crystallography, head the Facility as well as supervise regular operation of the equipment.
Services and Instrumentation
The Rigaku HighFlux HomeLab system is a complete home X-ray diffraction system enabling data collection on a wide range of protein crystal samples. The central component of the system is the MicroMax-007HF Microfocus rotating anode X-ray generator coupled to Varimax-HF Optics providing a focused, monochromatic, highly convergent beam with a focal spot size less than 0.1 mm. Auxiliary workstations are also available for data processing and solution calculations. This system has one of the highest brilliance outputs available for a home source. In addition, the system is a green alternative to other generators currently in use using approximately ~60% less energy per year than other generators.
The use of protein structures in the investigation of interesting biological, pharmaceutical and chemical questions has become increasingly prevalent over the past two decades. Structures determined by X-ray crystallography yield high resolution models of proteins and ligands for which the interactions of atoms can be visualized and interpreted. Examples of possible applications include:
- Biochemistry: structure-function studies
- Pharmaceutical Sciences: ligand binding and design
- Chemistry: protein and ligand design
- Materials Sciences: design of peptide nanoparticles
Training and Education
Training and expertise is available in crystal growth as well as the determination of three-dimensional structure of proteins and other macromolecular complexes.
Use of the Facility
Users will grow crystals of a protein or protein:ligand complex in order to begin an experiment. Assistance with crystal growth can be obtained from either of the Facility Co-Heads. Data collection is usually successful for single crystals that measure at least 0.1 mm on each side. The crystal will be frozen in a cryoprotectant solution and subjected to X-rays from the MicroMax system. Data are collected on an R-Axis IV image plate and processed using software available with the system. Structure determination can be carried out independently or in collaboration with the Facility Co-Heads.
Facility Use Fees:
Current service prices can be found by referring to the Rates/Budget Certification link or by clicking here.
All rates are subject to periodic review and change.