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Lecture

X-ray Free-electron Lasers: Biochemistry and Imaging

Description

This lecture covers the application of X-ray free-electron lasers in biochemistry, focusing on diffraction techniques before sample destruction, single-particle imaging, and chemical bond dynamics. It also explores high-pressure science and its relevance to various fields. Examples include bacteriorhodopsin retinal isomerization and the study of lattice dynamics in shock-compressed matter.

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Related concepts (32)

Powder diffraction

Powder diffraction is a scientific technique using X-ray, neutron, or electron diffraction on powder or microcrystalline samples for structural characterization of materials. An instrument dedicated to performing such powder measurements is called a powder diffractometer. Powder diffraction stands in contrast to single crystal diffraction techniques, which work best with a single, well-ordered crystal. Diffraction grating The most common type of powder diffraction is with x-rays, the focus of this article although some aspects of neutron powder diffraction are mentioned.

Diffraction

Diffraction is the interference or bending of waves around the corners of an obstacle or through an aperture into the region of geometrical shadow of the obstacle/aperture. The diffracting object or aperture effectively becomes a secondary source of the propagating wave. Italian scientist Francesco Maria Grimaldi coined the word diffraction and was the first to record accurate observations of the phenomenon in 1660.

Precession electron diffraction

Precession electron diffraction (PED) is a specialized method to collect electron diffraction patterns in a transmission electron microscope (TEM). By rotating (precessing) a tilted incident electron beam around the central axis of the microscope, a PED pattern is formed by integration over a collection of diffraction conditions. This produces a quasi-kinematical diffraction pattern that is more suitable as input into direct methods algorithms to determine the crystal structure of the sample.

Fraunhofer diffraction

In optics, the Fraunhofer diffraction equation is used to model the diffraction of waves when plane waves are incident on a diffracting object, and the diffraction pattern is viewed at a sufficiently long distance (a distance satisfying Fraunhofer condition) from the object (in the far-field region), and also when it is viewed at the focal plane of an imaging lens. In contrast, the diffraction pattern created near the diffracting object and (in the near field region) is given by the Fresnel diffraction equation.

X-ray crystallography

X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.

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