Radiation Damage in Protein Crystallography at X-ray Free-electron Lasers
نویسنده
چکیده
The ultrafast radiation damage begins with photoionization, followed by impact ionization by photoand Auger electrons. The ionization of atoms develops with time, ultimately causing lattice disorder and Coulomb explosion of the crystal. Due to very short pulse duration, it has been proposed that diffraction can be recorded before significant structural changes occur. This has been termed “diffraction-before-destruction”. However, achieving sufficient scattering signal for measuring nanocrystals or noncrystalline single particles requires higher power densities than those used in microcrystallography experiments.
منابع مشابه
Liquid sample delivery techniques for serial femtosecond crystallography.
X-ray free-electron lasers overcome the problem of radiation damage in protein crystallography and allow structure determination from micro- and nanocrystals at room temperature. To ensure that consecutive X-ray pulses do not probe previously exposed crystals, the sample needs to be replaced with the X-ray repetition rate, which ranges from 120 Hz at warm linac-based free-electron lasers to 1 M...
متن کاملSelenium single-wavelength anomalous diffraction de novo phasing using an X-ray-free electron laser
Structural information about biological macromolecules near the atomic scale provides important insight into the functions of these molecules. To date, X-ray crystallography has been the predominant method used for macromolecular structure determination. However, challenges exist when solving structures with X-rays, including the phase problem and radiation damage. X-ray-free electron lasers (X...
متن کاملSerial Femtosecond Crystallography
X-ray free-electron lasers produce brief flashes of X-rays that are of about a billion times higher peak brightness than achievable from storage ring sources. Such a tremendous jump in X-ray source capabilities, that came in 2009 when the Linac Coherent Light Source begun operations, was unprecedented in the history of X-ray science. Protein structure determination through the method of macromo...
متن کاملMultiwavelength anomalous diffraction at high x-ray intensity.
The multiwavelength anomalous diffraction (MAD) method is used to determine phase information in x-ray crystallography by employing anomalous scattering from heavy atoms. X-ray free-electron lasers (FELs) show promise for revealing the structure of single molecules or nanocrystals, but the phase problem remains largely unsolved. Because of the ultrabrightness of x-ray FEL, samples experience se...
متن کاملE pluribus unum, no more: from one crystal, many conformations.
Several distinct computational approaches have recently been implemented to represent conformational heterogeneity from X-ray crystallography datasets that are averaged in time and space. As these modeling methods mature, newly discovered alternative conformations are being used to derive functional protein mechanisms. Room temperature X-ray data collection is emerging as a key variable for sam...
متن کامل