Neutron protein crystallography

Based on its recently demonstrated success in identifying protons and bound water molecules, even at a relatively modest resolution of 2.0 Å, neutron protein crystallography carried out at room temperature has great potential to play a major role in the understanding of the mechanisms of enzymes (I. Tsyba & R. Bau, 'Neutron Diffraction Studies on Proteins', Chemtracts-Inorganic Chemistry 15, 233-257, 2002). The major reasons for the limited impact of neutron protein crystallography to date are the lack of suitable instruments and the limited flux at the presently available neutron sources, which means that very large crystals generally are required. This situation will change with the advent of the SNS, which will allow for unprecedented higher data collection rates.

On May 28, 2002 at the ACA meeting in San Antonio, a Steering Committee including scientific personnel with expertise in protein crystallography, enzymology, and neutron instrumentation was formed to look into the requirement of a dedicated neutron protein crystallography instrument at the Spallation Neutron Source (SNS). The SNS will be the world’s most intense source of neutrons when it becomes operational in 2006 at Oak Ridge, TN, USA. The Committee has adopted action items for the coming year including: (1) To hold focused workshops bringing the scientific community together, to discuss scientific problems that require neutron protein crystallography and to form of an SNS Instrument Development Team (IDT), and (2) To showcase the science using neutron protein crystallography at the Transactions Symposium at the 2003 ACA annual meeting in Cincinnati.

P. Thiyagarajan, from the ACA Newsletter, Fall 2002