protein_crystallRecent efforts in structural genomics have produced thousands of new proteins for study in structural biology and drug design projects. The number of new proteins available will continue to increase significantly in the next several years. However, the high throughput production of diffraction-quality crystals remains a major obstacle in structural proteomics, with success rates rarely exceeding 15% for soluble proteins. The CBSE provides several unique and powerful approaches for rapidly and efficiently determining optimum protein crystallization conditions in an efficient and cost effective manner.

The CBSE has adopted a parallel but knowledge-based approach for the crystallizing proteins. With minimal sample the CBSE can employ a host of techniques to solve the crystallization bottleneck. These techniques include custom in-house incomplete factorial screen designs, protein-protein interactions measurements, the utilization of in surfo and in meso nanoliter robotic methods, lipid synthesis, antibody fragment-mediated crystallization, and others.

The HTP crystallization screening facility minimizes the time and amount of protein needed by utilizing our custom designed instruments and a variety of commercially available equipment. This kind of capacity allows the CBSE to prepare thousands of experiments a day at the nano to microliter scale.

protein_crystallizationIn addition to design of many different constructs, the use of predictive algorithms, has shown to increase our success rate in optimizing solutions for diffraction-quality crystals. This technology supports our efforts to find new or optimize present conditions that improve crystal growth for both soluble and membrane proteins. Combining this technology with several in-house screen designs for different classes of proteins and other analytical measurements, such as the Second Virial Coefficient, create powerful predictors for crystallization that have yielded success for many difficult to crystallize proteins.

The CBSE can produce and purify your protein of interest for crystallization trials or work with purified protein sample sent to the facility. Our suite of technologies can produce new crystallization and/or optimize existing conditions to grow the high quality crystal needed for diffraction analysis. Expanded capabilities allow us to take the crystal from the lab and collect initial data sets at our in house X-ray facility or either collect the data one of two dedicated synchrotron beamlines at the Argonne Synchrotron Facility.