Abstract
The challenge in protein structure research is to visualize hydrogen positions at 8, resolution in biological structures. Neutrons are the ideal probe to detect hydrogen atoms in crystal structures, but in practice only a very limited number of protein structure papers using neutrons are published. The main drawbacks come from the large sample size required and the long data acquisition times in com- parison with X-ray measurements. Improvement in instrument performance and availability of more powerful neutron sources by next generation spallation-based facilities could solve these problems and, in complementarity to X-rays, open up the fieId of protein crystallography with neutrons.
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