‘Mail-in’ Crystallography at Brookhaven National Laboratory Highlighted in Nature


Scientists with the protein crystallography (PX) program at Brookhaven National Laboratory (BNL) have solved a major obstacle to wider use of synchrotron light sources by the structural biology community. Synchrotron radiation has become essential for solving structures of proteins and other biological macromolecules and complexes using x-ray diffraction. Yet there are only five of these facilities in the U.S. where such experiments can be done. Thus most scientists must travel a considerable distance to carry out a structural study, often spending more time on travel than on the actual experiment. Over the past four years Robert Sweet and Howard Robinson of BNL’s Biology Department and their colleagues have developed a service by which scientists can send frozen crystals to Brookhaven and have the local BNL staff carry out the PX data collection at the National Synchrotron Light Source (NSLS). The service is described in an article in the June 19, 2003, issue of the widely-read journal Nature. The article points out that some 50 research groups are using this service annually, half of them being molecular biologists with little previous crystallography experience. The service enables these scientists to get results in weeks instead of having to wait for months for an opportunity to run experiments at the NSLS themselves. In turn, the available beam time is used much more efficiently, since expert BNL staff are running the experiments instead of novice users. The article notes that the European Synchrotron Radiation Facility is now offering a similar service and that several other synchrotrons in the United States are considering setting one up.

Principal Investigator(s)

Robert Sweet
Brookhaven National Laboratory


Schmidt, T., 2003. “The Crystal’s in the Mail,” Nature 423,799–800. DOI: 10.1038/423799a.