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A powder X-ray diffractometer in motion. X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract in specific directions.
Isomorphous replacement (IR) is historically the most common approach to solving the phase problem in X-ray crystallography studies of proteins.For protein crystals this method is conducted by soaking the crystal of a sample to be analyzed with a heavy atom solution or co-crystallization with the heavy atom.
X-ray reflectivity is an analytical technique for determining thickness, roughness, and density of single layer and multilayer thin films. Wide-angle X-ray scattering (WAXS), a technique concentrating on scattering angles 2θ larger than 5°. Spectrum of various inelastic scattering processes that can be probed with inelastic X-ray scattering ...
The term WAXS is commonly used in polymer sciences to differentiate it from SAXS but many scientists doing "WAXS" would describe the measurements as Bragg/X-ray/powder diffraction or crystallography. Wide-angle X-ray scattering is similar to small-angle X-ray scattering (SAXS) but the increasing angle between the sample and detector is probing ...
Multi-wavelength anomalous diffraction (sometimes Multi-wavelength anomalous dispersion; abbreviated MAD) is a technique used in X-ray crystallography that facilitates the determination of the three-dimensional structure of biological macromolecules (e.g. DNA, drug receptors) via solution of the phase problem.
Single-wavelength anomalous diffraction (SAD) is a technique used in X-ray crystallography that facilitates the determination of the structure of proteins or other biological macromolecules by allowing the solution of the phase problem.
Molecular replacement (MR) [1] is a method of solving the phase problem in X-ray crystallography.MR relies upon the existence of a previously solved protein structure which is similar to our unknown structure from which the diffraction data is derived.
A Bernal chart (bər′nal ′chärt) in crystallography, is a chart used for indexing X-ray diffraction photographs from single crystals. From such a chart may be read the axial and radial cylindrical coordinates of that point in reciprocal space which corresponds to any particular X-ray reflection. [1]