Protons in proteins discussed in Grenoble

A joint ILL/EMBL workshop was held in Grenoble from January 25 to 27, 2001 to discuss the structural role of hydrogen in biological function and to look objectively at the contribution that neutron protein crystallography can make to the field, particularly in light of the information now available from complementary techniques, such as high resolution X-ray crystallography and NMR. Protons in Proteins: Biological Applications of Neutron Diffraction was opened by Venki Ramakrishnan (Cambridge), who discussed the role and particular achievements of neutron scattering in biology and stressed that neutrons should continue to focus upon important biological problems. Sean McSweeny (ESRF) described how recent advances in X-ray cryocrystallography can locate hydrogen atoms in protein structures determined at atomic resolution, but warned of radiation induced artifacts. Joseph Parello (Montpellier) showed how protons could be located by a combination of such high resolution (0.9Å) X-ray work and NMR in the EF-hand protein, parvalbumin. The new generation of neutron protein crystallography instrumentation was reviewed. Dean Myles (EMBL) presented highlights of neutron protein structures, large and small, determined using the quasi-Laue instrument LAD1 at ILL and Nobuo Niimura (JAERI) described work on rubredoxin and myoglobin using the BIX-3 diffractometer at JAERI. Benno Schoenborn (Los Alamos) presented the newly completed TOF Laueinstrument for macromolecular diffraction at LANSCE, which had received first neutrons only weeks before!.