A New Tool for Pharmaceutical Companies Technology Transfer from Cornell University
Product News Mar 21, 2014
ADC has announced the market availability of a High Pressure Cryo-Cooler for X-Ray Crystallography (HPC-201). All qualifications have been successfully met as well as the passing of safety and testing.
The original concept was licensed from Cornell University through its Cornell Center for Technology Enterprise & Commercialization (CCTEC).
The method of high pressure cryo-cooling is used to obtain both intensity and phase information from a single protein crystal, enabling the user to solve the protein’s crystal structure.
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 effective technique in the field of structural biology; out of the approximately 35,000 protein structures solved, x-ray crystallography is responsible for about 29,000.
The promise of structural biology to improve human healthcare is great, and any method or device that can speed the solving of protein structures will contribute to fulfilling that promise.
This device’s fundamental design is based on a process developed by Prof. Sol M. Gruner (http://bigbro.biophys.cornell.edu/) and Dr. Chae Un Kim of Cornell University and protected by; US Patent No. 8,030,449. This exciting new technology enables the simultaneous capture of both amplitude and phase information from a single anomalous diffraction (SAD) of a cryo-cooled protein crystal, thereby providing sufficient data to solve the crystal structure of a protein with a previously unknown structure.
Flash-freezing at atmospheric pressure requires the use of cryoprotectants. Finding the right cyroprotectant for 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 first funded by The National Institutes of Health (NIH). Through its National Institute of General Medical Sciences, NIH funds MacCHESS for two purposes: core research as motivated by the important biomedical problems and support to all structural biologists making use of the Cornell High Energy Synchrotron Source (CHESS) facility for crystallographic and small-angle X-ray scattering experiments, as well as for novel experiments requiring special equipment and staff assistance not readily available at other synchrotron sources.