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DALI Extending the capacity and capability for neutron macromolecular crystallography

Characteristics

Guide hall n°1, cold guide H141
Data Collection Method
Quasi-Laue Neutron Velocity Selector
Typical neutron λ 3.35 to 3.70 Å (with NVS@25K rpm)
Collimation
Pinholes 0.5 to 2.9 mm
Flux at specimen
(λ-centre = 3.53 Å; δλ/λ ~10%) ~1 x 108n cm-2s-1
Detector
Cylindrical drum with internal neutron-sensitive image plates and read/erase system
Neutron image plate Gd2O3doped BaF(Br.I):Eu2+
Radius 160 mm
Length 400 mm
Active area 1000 x 400 mm2
Pixel size 100, 200, 400 µm2
Sample environment
(1) Ambient or (2) Oxford Cryosystems 'COBRA' cryostream (down to 80K)

A huge advance for high-resolution studies of large proteins

In October 2025, a completely new neutron-sensitive cylindrical image plate detector was built and installed on DALI. Neutron diffraction tests and analyses were performed using crystals of proteins covering a wide range of molecular weights, from the very small (6 kDa) to the very large (271 kDa). The results show that the LADI-III and DALI macromolecular crystallography diffractometers are highly complementary.

LADI-III delivers higher quality diffraction data for small to medium-sized proteins (5-70 kDa) and DALI, with its new detector and narrow bandwidth velocity selector, now delivers diffraction data of higher quality for large proteins (70-150 kDa). In addition, the tests indicate that DALI can even be used to study very large proteins (>150 kDa) that were previously out of range. This represents a step change in capabilities for neutron protein crystallography research and further cements the ILL’s position as world-leading in the field.

Below shows a 16-hour exposure from a crystal of 105 kDa protein (LecA/PheGal complex, unit-cell, a = 74, b = 111, c = 113 Å / P212121). Complete data set collected to 2.0 Å resolution. [LecA protein is a virulence factor of the pathogenic bacteria Pseudomonas aeruginosa. Specific ligands - molecules binding to specific sites of the protein to form molecular complexes – can counteract P. aeruginosa infections if they block specific protein sites involved in the process.]