 | Student Christina Hueneke of the Midwest Center for Structural Genomics overseeing a protein cloning robot. The protein cloning robot was designed as part of an effort to exponentially increase the output of a traditional web lab. Part of the center's goal is to cut the average cost of analyzing a protein from $200,000 to $20,000 and to slash the average time from months to days and hours. HIgh-res image (2.66 MB JPEG)
Low-res image (377 KB JPEG) Credit: Midwest Center for Structural Genomics |
 | Irina Dementieva, a biochemist, and Youngchang Kim, a biophysicist and crystallographer, workwith the first robot if its type in the U.S. to automate protein prufication. The robot, which is housed in a refrigerator, is an integral part of the Midwest Structural Genomics Center's plan to automate the protein crystallography process. High-res image (949 KB JPEG)
Low-res image (308 KB JPEG) Credit: Midwest Center for Structural Genomics |
| Cell-free protein synthesizers
Both instruments were developed by CellFree Sciences, of Yokohama, Japan. The instrument on the left, the GeneDecoder 1000, can generate 384 proteins from their corresponding genes, or gene fragments, overnight. It is used to screen for properties such as level of protein production and degree of solubility. The instrument on the right, the Protemist Protein Synthesizer, is used to generate the larger amounts of protein needed for protein structure determinations. High-res image (3.38 MB JPEG)
Low-res image (291 KB JPEG) Credit: Center for Eukaryotic Structural Genomics |
| CESG Protein Purification Facility
The Center for Eukaryotic Structural Genomics protein purification facility is responsible for purifying all recombinant proteins produced by the center. The facility performs several purification steps, monitors the quality of the processes, and stores information about the biochemical properties of the purified proteins in the facility database. High-res image (1.82 MB JPEG)
Low-res image (265 KB JPEG) Credit: Center for Eukaryotic Structural Genomics |
| Varian Unity Inova 900 MHz, 21.1 T standard bore magnet Nuclear Magnetic Resonnance (NMR) spectrometer
NMR spectroscopy provides data used to determine the structures of proteins in solution, rather than in crystal form, as in X-ray crystallography. The technique is limited to smaller proteins or protein fragments in a high throughput approach. High-res image (2.25 MB JPEG)
Low-res image (285 KB JPEG) Credit: Center for Eukaryotic Structural Genomics |
| Capillary Protein Crystallization Robot ACAPELLA
This robot grows protein crystals, freezes them, and centers them without manual intervention. The close up is a view of one of the dispensers used for dispensing proteins and reagents. High-res image (3.05 MB JPEG)
Low-res image (172 KB JPEG) Credit: Structural Genomics of Pathogenic Protozoa Consortium |
| Multi-probe sonicator
This instrument was designed by Shawn McGuire, and is used to break open bacterial cells in the protein production step of protein structure determination. High-res image (1.17 MB JPEG)
Low-res image (239 KB JPEG) Credit: Structural Genomics of Pathogenic Protozoa Consortium |
 | From genes to structures The PSI will determine the three-dimensional shapes of a wide range of proteins by solving the structures of representative members of each protein family found in nature. The collection of structures will serve as a valuable resource for biomedical research scientists. High-res image (100 KB JPEG)
Low-res image (20 KB JPEG) Credit: National Institute of General Medical Sciences |
 | The JCSG HT protein structure determination pipeline The JCSG has pioneered development of technologies for many steps from gene to structure which have been integrated into a HT pipeline that includes all of the steps from target selection, parallel expression, protein purification, automated crystallization trials, automated crystal screening, structure determination, validation, and publication. High-res image (1.04 MB JPEG)
Low-res image (215 KB JPEG) Credit: Joint Center for Structural Genomics |
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 | The Southeast Collaboratory for Structural Genomics Chromium X-ray source In the determination of protein structures by X-ray crystallography, this unique soft (l = 2.29Å) X-ray source is used to collect anomalous scattering data from protein crystals containing light atoms such as sulfur, calcium, zinc and phosphorous. This data can be used to image the protein. High-res image (1.76 MB JPEG)
Low-res image (265 KB JPEG) Credit: The Southeast Collaboratory for Structural Genomics
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| The Advanced Photon Source (APS) at Argonne National Lab The intense X-rays produced by synchrotrons such as the APS are ideally suited for protein structure determination. Using synchrotron X-rays and advanced computers scientists can determine protein structures at a pace unheard of decade ago. High-res image (4.26 MB JPEG)
Low-res image (362 KB JPEG) Credit: Southeast Collaboratory for Structural Genomics |
 | Automated crystal screening system Automated crystal screening systems such as the one shown here are becoming a common feature at synchrotron and other facilities where high throughput crystal structure determination is being carried out. These systems rapidly screen samples to identify the best candidates for further study. High-res image (3.74 MB JPEG)
Low-res image (345 KB JPEG) Credit: Southeast Collaboratory for Structural Genomics
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| Robot transferring 96 purification columns to vacuum manifold for subsequent purification procedures Credit: The Northeast Collaboratory for Structural Genomics |
 | Automated 8-channelpipet head loading proteins onto purification columns Credit: The Northeast Collaboratory for Structural Genomics |
| Automated mounting of protein crystals for X-ray crystallography using micromachined silicon "shovels" Credit: The Northeast Collaboratory for Structural Genomics |
