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www.adc9001.com HPC-201 HigH Pressure Cryo-Cooler or X-ray CrystallograPHy Pharmaceutical companies currently use x-ray crystallography to determine exactly how drug lead compounds and their protein targets interact. To date, x-ray crystallography is the most eective technique in the eld o structural biology; out o the approximately 35,000 protein structures solved, x-ray crystallography is responsible or about 29,000. The promise o structura l biology to improve human health is great, and any method or device that can speed the solving o protein structures will contribute to ullling that promise. Cornell University developed a novel method to cryo-cool protein crystals without the need or penetrative cryoprotectants. The method involves mounting protein crystals in a cryoloop with a thin coating o oil, pressurizing the crystal up to 200 MPa (200 0 atm) in He gas, cooling the crystal under pressure, and then releasing the pressure. This process results in dramatic improveme nt in diraction quality in terms o diraction resolution and crystal mosaicity. This device’s undamental design is based on a process developed and patented by Cornell University scientists Pro. Sol M. Gru ner (http://bigbro.biophys.cornell.edu/ ) and Dr. Chae Un Kim; US Patent No. 8,030,449. Flash-reezing at atmospheric pressure typically requires the use o cryoprotectants. Finding the right cyroprotectant or each sample type can be a long, trial-and- error process. The High Pressure Cryo-Cooler eliminates the need to use cryoprotectants and produces superior results. The project was rst unded by The National Institutes o Health. The National Institutes o Health (NIH), through its National Institute o General Medical Sciences (NIGMS), unds MacCHESS or two purposes: core research as motivated by important biomedical problems and support to all structural biologists making use o the CHESS acility or crystallographic and small- angle X-ray scattering experiments, as well as or novel experiments requiring special equipment and sta assistance not readil y available at other synchrotron sources. Pc Once a protein crystal has been picked up using a loop, or similar device, the crystal is analyzed using x-rays. Unortunately, a typical protein crystal at room temperature survives only a raction o the x-ray dose required or a complete high resolution data set beore it becomes irrevocably radiation-damaged. To inhibit the radiation damage, protein crystals are typically ash coole d at atmospheric pressure by plunging them into liquid nitrogen (77 K or -196 °C). Cryocooling also reduces the thermal motion within the crystal, enabling the collection o higher quality data. Freezing protein crystals successully and without physical damage, however, is a tricky business. Proteins crystals orm in an aqueous solution and can contain 50 percent, or more, water by weight. As anyone knows who is lucky enough to be by a northern lake on a rigid night early in the winter, as the ice noisily heaves and cracks, reezing water expands with great orce—more than enough to damage the crystals one is trying to protect. The goal o ash reezing is or the water to orm amorphous ice rather than crystalline ice. Cryoprotectants are typically added to promote this result. Unortunately, since each protein is unique, a specic cryoprotectant must be ormulated or each, a task that proves difcult or impossible in many cases. Proessor Sol Gruner, and Dr. Chae Un Kim’s innovations have eliminated the need or cryoprotectants in many cases while increasing cryocooled protein crystal quality. Instead o reezing protein crystals at atmospheric pressure, they cryo-cool the ir protein crystals under high pressure. Under these conditions, the water turns into a higher density orm o amorphous ice, whic h minimizes crystal disruption. This process is simple in concept—pressurize a protein crystal in helium at room temperature up to between 100 and 400 MPa (about 14,500 to 58,000 psi), cryocool the crystal to 77 K, then release the pressure while maintaining the low temperature— but complicated in practice, due to the high pressures involved. Protein crystal structure is solved by determining the repetitive three-dimensional electron density distribution o protein molecules in a crystalline arrangement. Each crystal reection has an intensity (amplitude) and phase, and both are needed to generate a protein structure. The inormation obtained rom an x-ray diraction experiment provides intensity data directly. In some cases, it is possible to use “anomalous diraction” to also obtain phases. With single-wavelength anomalous diraction
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