IUCr journals

High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase

Acta Cryst. (2005). D61, 1413–1417

[Neutron protein crystallography]
Full deuteration of human aldose reductase (MW = 36 kDa) significantly improved the neutron diffraction signal/noise ratio compared with that obtained with hydrogen/deuterium partially exchanged samples. Consequently, a good quality data set (2.2 Å resolution at room temperature) was collected on the LADI diffractometer at the ILL neutron source (France), with a crystal volume (0.15 mm3) radically smaller than usual for neutron diffraction studies. Deuterium atoms are clearly visible in neutron scattering density maps at 2.2 Å resolution (see proline 13, 2FoFc map, 1.5 r.m.s. contour).

I. Hazemann, M. T. Dauvergne, M. P. Blakeley, F. Meilleur, M. Haertlein, A. Van Dorsselaer, A. Mitschler, D. A. A. Myles and A. Podjarny