Corporate Banner
Satellite Banner
Scientific Community
Become a Member | Sign in
Home>News>This Article

A New Tool for Pharmaceutical Companies Technology Transfer from Cornell University

Published: Friday, March 21, 2014
Last Updated: Friday, March 21, 2014
Bookmark and Share
High pressure cryo-cooler for X-ray crystallography from ADC.

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 ( 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.

Further Information
Access to this exclusive content is for Technology Networks Premium members only.

Join Technology Networks Premium for free access to:

  • Exclusive articles
  • Presentations from international conferences
  • Over 2,800+ scientific posters on ePosters
  • More than 4,000+ scientific videos on LabTube
  • 35 community eNewsletters

Sign In

Forgotten your details? Click Here
If you are not a member you can join here

*Please note: By logging into you agree to accept the use of cookies. To find out more about the cookies we use and how to delete them, see our privacy policy.

Scientific News
A New Way to Look at MOFs
International study challenges prevailing view on how metal organic frameworks store gases.
Major Advance in Crystal Structure Prediction Methods
The Cambridge Crystallographic Data Centre (CCDC) announces that the results of its 6th blind test of crystal structure prediction methods demonstrate significant advancement in in comparison with previous tests.
Protein Structure Discovery Opens Window on Basic Life Process
Biochemists at Oregon State University have made a fundamental discovery about protein structure that sheds new light on how proteins fold, which is one of the most basic processes of life.
Clearest Ever Images of Enzyme that Plays Key Roles in Aging, Cancer
UCLA-led research on telomerase could lead to new strategies for treating disease
New Approach to Treating Heparin-induced Blood Disorder
A potential treatment for a serious clotting condition that can strike patients who receive heparin to treat or prevent blood clots may lie within reach by elucidating the structure of the protein complex at its root.
Escape Prevention
Studying flu virus structure brings us a step closer to a permanent vaccine.
Structure of Protein at Root of Muscular Disease Decoded
Researchers at Rice University and Baylor College of Medicine have unlocked the structural details of a protein seen as key to treating a neuromuscular disease.
A Natural Light Switch
MIT scientists identify and map the protein behind a light-sensing mechanism.
First Complete Structural Study Of A Pegylated Protein
Significant data obtained at NUI Galway reports first crystal structure of a protein modified with a single PEG chain.
Cellular Contamination Pathway for Heavy Elements Identified
Berkeley Lab scientists find that an iron-binding protein can transport actinides into cells.
Skyscraper Banner

Skyscraper Banner
Go to LabTube
Go to eposters
Access to the latest scientific news
Exclusive articles
Upload and share your posters on ePosters
Latest presentations and webinars
View a library of 1,800+ scientific and medical posters
2,800+ scientific and medical posters
A library of 2,500+ scientific videos on LabTube
4,000+ scientific videos