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DALI Extending the capacity and capability for neutron macromolecular crystallography

DALI - Extending the capacity and capability for neutron macromolecular crystallography

DALI - A quasi-Laue diffractometer for large proteins

To extend the capabilities and capacity for neutron macromolecular crystallography at the ILL, a second quasi-Laue diffractometer DALI has been commissioned at H141 as part of the ILL Endurance Programme. DALI utilizes a neutron velocity selector to provide higher transmission and a narrower bandwidth (δλ/λ ~10%) than LADI-III, both required to extend capabilities to the study of larger proteins.

DALI allows high-resolution (~1.8 - 2.5 Å) studies of large proteins (>70kDa), in order to locate hydrogen/deuterium (H/D) atoms and protons/deuterons (H+/D+) of special interest, revealing important information on protonation, H-bonding and hydration. Neutron macromolecular crystallography is unique in its ability to provide these invaluable details at room-temperature, and without radiation damage.

Applications

Neutron macromolecular crystallography projects typically aim to address questions concerning:

  • Enzyme mechanisms
  • Small-molecule (e.g. drug, ligand) binding interactions
  • Rational drug-design

Instrument layout

DALI uses a large cylindrical area detector composed of neutron-sensitive image-plates, which completely surround the crystal and allows large numbers of reflections to be recorded simultaneously. Data are collected using quasi-Laue methods in order to provide a rapid survey of reciprocal space, while reducing the background on the detector compared to use of the full white beam.