Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.

Abstract

A crystallogenesis study of human transthyretin using the counter-diffusion method is described as an alternative to conventional convective vapour diffusion and batch approaches for protein crystallization. The X-ray diffraction results show systematic trends that exhibit unique patterns of crystallization and high crystal quality as well as a remarkable degree of coherence within extended crystal rods that wholly fill the capillaries used. Preliminary neutron diffraction data have been recorded from a number of these samples, validating the feasibility of this methodology for neutron crystallography.