Do Heon Gu, Dong Tak Jeong, Cheolsoo Eo, Pil Won Seo, Jeong Sun Kim, Suk Youl Park
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引用次数: 0
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.
期刊介绍:
Synchrotron radiation research is rapidly expanding with many new sources of radiation being created globally. Synchrotron radiation plays a leading role in pure science and in emerging technologies. The Journal of Synchrotron Radiation provides comprehensive coverage of the entire field of synchrotron radiation and free-electron laser research including instrumentation, theory, computing and scientific applications in areas such as biology, nanoscience and materials science. Rapid publication ensures an up-to-date information resource for scientists and engineers in the field.