Structure solution based on the weak anomalous signal from native (protein and
DNA) crystals is increasingly being attempted as part of synchrotron
experiments. Maximizing the measurable anomalous signal by collecting
diffraction data at longer wavelengths presents a series of technical challenges
caused by the increased absorption of X-rays and larger diffraction angles. A
new beamline at Diamond Light Source has been built specifically for collecting
data at wavelengths beyond the capability of other synchrotron macromolecular
crystallography beamlines. Here, the theoretical considerations in support of
the long-wavelength beamline are outlined and the in-vacuum design of the
endstation is discussed, as well as other hardware features aimed at enhancing
the accuracy of the diffraction data. The first commissioning results,
representing the first in-vacuum protein structure solution, demonstrate the
promising potential of the beamline.
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