Abstract
Synchrotron serial crystallography (SSX) is an emerging method for determining crystal structure at room temperature using synchrotron radiation facilities. Despite the various approaches available, reducing sample consumption, removing mother liquid from crystal solution, soaking small molecules for protein-ligand complex structure and prevention of sample dehydration are still challenging problems to be overcome in SSX. Therefore, we have developed a new flip-type fixed-target SSX sample holder for conventional protein crystallography beamlines based on nylon mesh and kapton film. The potential of the flip-holder was evaluated in an SSX experiment with lysozyme crystals at room temperature. About 19600 diffraction images were collected during 40 minutes using a repetition rate of 10 Hz at the 11C beamline of the Pohang Accelerator Laboratory, and the crystal structure of lysozyme was determined at 1.89 Å resolution. This straightforward flip-holder can be used in synchrotron beamlines for routine crystallography.
Published Version
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