QIAGEN N.V. has announced that it has entered a strategic agreement with the Joint Center for Structural Genomics (JCSG), one of the 4 PSI Structural Genomics Production Centers, providing protein crystallographers with a set of proven crystallization screens that have been assembled from analysis of hundreds of thousands of crystallization experiments.
Protein crystallography is a complex process used to determine the three-dimensional structure of proteins. By elucidating the structure of proteins, scientists can discover new drugs that more effectively target disease.
To generate crystals, protein samples undergo a crystallization screening step, in which protein samples are combined in multiple reactions with different chemical solutions.
This set of 384 conditions - split into four screens of 96 conditions - was previously provided by QIAGEN as a customized product and will be supplied to the wider market as The JCSG Core Suites I-IV. The screens are the result of analyzing over 500,000 high-throughput crystallization experiments performed at the JCSG. The 384 crystallization conditions that provided the highest hit rates in initial screening were chosen to form the screens.
"Improving initial sample preparation screens for crystallization is a continuous effort of the crystallographic community", said Kai te Kaat, Global Business Director Proteins at QIAGEN. "These new screens are the result of mining the vast database of crystallization experiments performed by the JCSG. We are proud to have been selected by the JCSG as their partner to commercialize these screens to the entire crystallographic community in QIAGEN's proprietary sample technology formats."
The JCSG has chosen QIAGEN as their main supplier of crystallization screens for its quality and customer orientation in the development process. "I am delighted that QIAGEN markets these JCSG screens", said Professor Ian Wilson, Principal Investigator of the JCSG. "It enables the fruits of the NIH Protein Structure Initiative to become available to all structure biologists and allow them the opportunity to enhance their own individual success rates in protein crystallization."