Long-wavelength protein crystallography at Diamond Light Source
نویسندگان
چکیده
منابع مشابه
Chemical Crystallography at the Advanced Light Source
Chemical crystallography at synchrotrons was pioneered at the Daresbury SRS station 9.8. The chemical crystallography beamlines at the Advanced Light Source seek to follow that example, with orders of magnitude more flux than a lab source, and various in situ experiments. This article attempts to answer why a chemist would require synchrotron X-rays, to describe the techniques available at the ...
متن کاملAt-wavelength metrology of x-ray optics at Diamond Light Source
Modern, third-generation synchrotron radiation sources provide coherent and extremely bright beams of X-ray radiation. The successful exploitation of such beams depends to a significant extent on imperfections and misalignment of the optics employed on the beamlines. This issue becomes even more critical with the increasing use of active optics, and the desire to achieve diffraction-limited and...
متن کاملIn-vacuum long-wavelength macromolecular crystallography.
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 Diam...
متن کاملA step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10-5 mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted cr...
متن کاملTowards long-wavelength protein crystallography: keeping a protein crystal frozen in vacuum
There is growing interest to explore the long-wavelength X-ray domain for macromolecular crystallography (MX) experiments but there are a number of practical issues that make these experiments difficult to perform. In this article we study several aspects related to cooling a protein crystal in a vacuum environment. We investigated thermal contact conductance (TCC) of copper-copper joints and d...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations and Advances
سال: 2019
ISSN: 2053-2733
DOI: 10.1107/s2053273319088119