Results 21 to 30 of about 7,626 (235)

Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation

open access: yesIUCrJ, 2017
Crystal structure determination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render
Jose M. Martin-Garcia   +29 more
doaj   +3 more sources

Pink-beam serial crystallography

open access: yesNature Communications, 2017
Serial X-ray crystallography (SX) is used for data collection at X-ray Free Electron Lasers. Here the authors show that a polychromatic “pink” synchrotron X-ray beam can be used for SX, which is useful when crystal supply is limited and will allow time ...
A. Meents   +19 more
doaj   +2 more sources

Serial crystallography using synchrotron radiation [PDF]

open access: yesIUCrJ, 2014
A brief history is given of how X-ray diffraction data from crystals have been recorded. Today there are new possibilities, spawned by the availability of free electron lasers that produce powerful femtosecond long X-ray pulses.
Michael G. Rossmann
doaj   +3 more sources

Best practices for time-resolved serial synchrotron crystallography. [PDF]

open access: yesActa Crystallogr D Struct Biol, 2022
With recent developments in X-ray sources, instrumentation and data-analysis tools, time-resolved crystallographic experiments, which were originally the preserve of a few expert groups, are becoming simpler and can be carried out at more radiation sources, and are thus increasingly accessible to a growing user base. However, these experiments are just
Schulz EC   +3 more
europepmc   +6 more sources

Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins

open access: yesIUCrJ, 2019
An approach is demonstrated to obtain, in a sample- and time-efficient manner, multiple dose-resolved crystal structures from room-temperature protein microcrystals using identical fixed-target supports at both synchrotrons and X-ray free-electron lasers
Ali Ebrahim   +14 more
doaj   +3 more sources

Increasing X-ray energy improves data quality in serial crystallography [PDF]

open access: yesJournal of Synchrotron Radiation
Serial synchrotron crystallography (SSX) enables structure determination from microcrystals under near-physiological, room-temperature conditions but is limited in part due to the inevitable onset of radiation damage.
Do-Heon Gu   +4 more
doaj   +2 more sources

Serial crystallography on in vivo grown microcrystals using synchrotron radiation

open access: yesIUCrJ, 2014
Crystal structure determinations of biological macromolecules are limited by the availability of sufficiently sized crystals and by the fact that crystal quality deteriorates during data collection owing to radiation damage. Exploiting a micrometre-sized
Cornelius Gati   +13 more
doaj   +6 more sources

Novel fixed-target serial crystallography flip-holder for macromolecular crystallography beamlines at synchrotron radiation sources

open access: yesJournal of Synchrotron Radiation
Synchrotron serial crystallography (SSX) is an emerging method for determining crystal structure at room temperature using synchrotron radiation facilities.
Do-Heon Gu   +5 more
doaj   +3 more sources

Room-temperature serial synchrotron crystallography of the human phosphatase PTP1B. [PDF]

open access: yesActa Crystallogr F Struct Biol Commun, 2023
Room-temperature X-ray crystallography provides unique insights into protein conformational heterogeneity, but obtaining sufficiently large protein crystals is a common hurdle. Serial synchrotron crystallography (SSX) helps to address this hurdle by allowing the use of many medium- to small-sized crystals.
Sharma S, Ebrahim A, Keedy DA.
europepmc   +3 more sources

Room-temperature serial synchrotron crystallography of Drosophila cryptochrome. [PDF]

open access: yesActa Crystallogr D Struct Biol, 2022
Fixed-target serial crystallography allows the high-throughput collection of diffraction data from small crystals at room temperature. This methodology is particularly useful for difficult samples that have sensitivity to radiation damage or intolerance to cryoprotection measures; fixed-target methods also have the added benefit of low sample ...
Schneps CM, Ganguly A, Crane BR.
europepmc   +3 more sources

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