Crystallography is the experimental science of determining the arrangement of atoms in crystalline solids. Crystallography is a fundamental subject in the fields of materials science and solid-state physics. The word "crystallography" is derived from the Greek words κρύσταλλος (krystallos) "clear ice, rock-crystal", with its meaning extending to all solids with some degree of transparency, and γράφειν (graphein) "to write". In July 2012, the United Nations recognised the importance of the science of crystallography by proclaiming that 2014 would be the International Year of 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.
In X-ray crystallography, wide-angle X-ray scattering (WAXS) or wide-angle X-ray diffraction (WAXD) is the analysis of Bragg peaks scattered to wide angles, which are caused by sub-nanometer-sized structures. It is an X-ray-diffraction method and commonly used to determine a range of information about crystalline materials. 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.
A free-electron laser (FEL) is a light source producing extremely brilliant and short pulses of radiation. An FEL functions and behaves in many ways like a laser, but instead of using stimulated emission from atomic or molecular excitations, it employs relativistic electrons as a gain medium. Radiation is generated by a bunch of electrons passing through a magnetic structure. In an FEL, this radiation is further amplified as the radiation re-interacts with the electron bunch such that the electrons start to emit coherently, thus allowing an exponential increase in overall radiation intensity.
Photosystem II is the first protein complex in the light-dependent reactions of oxygenic photosynthesis. It is located in the thylakoid membrane of plants, algae, and cyanobacteria. Within the photosystem, enzymes capture photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. The energized electrons are replaced by oxidizing water to form hydrogen ions and molecular oxygen.
In physics, the phase problem is the problem of loss of information concerning the phase that can occur when making a physical measurement. The name comes from the field of X-ray crystallography, where the phase problem has to be solved for the determination of a structure from diffraction data. The phase problem is also met in the fields of imaging and signal processing. Various approaches of phase retrieval have been developed over the years.
Electron crystallography is a method to determine the arrangement of atoms in solids using a transmission electron microscope (TEM).
Diffraction topography is a quantum beam imaging technique based on Bragg diffraction. Diffraction topographic images ("topographies") record the intensity profile of a beam of X-rays diffracted by a crystal. A topography thus represents a two-dimensional spatial intensity mapping of reflected X-rays, i.e. the spatial fine structure of a Laue reflection. This intensity mapping reflects the distribution of scattering power inside the crystal; topographs therefore reveal the irregularities in a non-ideal crystal lattice. X-ray diffraction topography is one variant of X-ray imaging, making use of diffraction contrast rather than absorption contrast which is usually used in radiography and computed tomography (CT). Topography is exploited to a lesser extends with neutrons and other quantum beams. In the electron microscope community, such technique is called dark field imaging or diffraction contrast imaging.
The European X-Ray Free-Electron Laser Facility is an X-ray research laser facility commissioned during 2017. The first laser pulses were produced in May 2017 and the facility started user operation in September 2017. The international project with twelve participating countries; nine shareholders at the time of commissioning, later joined by three other partners, is located in the German federal states of Hamburg and Schleswig-Holstein. A free-electron laser generates high-intensity electromagnetic radiation by accelerating electrons to relativistic speeds and directing them through special magnetic structures. The European XFEL is constructed such that the electrons produce X-ray light in synchronisation, resulting in high-intensity X-ray pulses with the properties of laser light and at intensities much brighter than those produced by conventional synchrotron light sources.
Acta Crystallographica is a series of peer-reviewed scientific journals, with articles centred on crystallography, published by the International Union of Crystallography (IUCr). Originally established in 1948 as a single journal called Acta Crystallographica, there are now six independent Acta Crystallographica titles:
Multiple isomorphous replacement (MIR) 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. The addition of the heavy atom to the structure should not affect the crystal formation or unit cell dimensions in comparison to its native form, hence, they should be isomorphic.
A crystallographic database is a database specifically designed to store information about the structure of molecules and crystals. Crystals are solids having, in all three dimensions of space, a regularly repeating arrangement of atoms, ions, or molecules. They are characterized by symmetry, morphology, and directionally dependent physical properties. A crystal structure describes the arrangement of atoms, ions, or molecules in a crystal.
Protein crystallization is the process of formation of a regular array of individual protein molecules stabilized by crystal contacts. If the crystal is sufficiently ordered, it will diffract. Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye.
John Charles Howorth Spence ForMemRS HonFRMS was Richard Snell Professor of Physics at Arizona State University and Director of Science at the National Science Foundation BioXFEL Science and Technology Center.
Quantum crystallography is a branch of crystallography that investigates crystalline materials within the framework of quantum mechanics, with analysis and representation, in position or in momentum space, of quantities like wave function, electron charge and spin density, density matrices and all properties related to them. Like the quantum chemistry, Quantum crystallography involves both experimental and computational work. The theoretical part of quantum crystallography is based on quantum mechanical calculations of atomic/molecular/crystal wave functions, density matrices or density models, used to simulate the electronic structure of a crystalline material. While in quantum chemistry, the experimental works mainly rely on spectroscopy, in quantum crystallography the scattering techniques play the central role, although spectroscopy as well as atomic microscopy are also sources of information.
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization.
Microcrystal electron diffraction, or MicroED, is a CryoEM method that was developed by the Gonen laboratory in late 2013 at the Janelia Research Campus of the Howard Hughes Medical Institute. MicroED is a form of electron crystallography where thin 3D crystals are used for structure determination by electron diffraction.
This is a timeline of crystallography.
Petra Fromme is a German-American chemist who is Director of the Biodesign Center for Applied Structural Discovery and Regents Professor at the Arizona State University. Her research considers the structure-to-function relationship of the membrane proteins involved with infectious diseases and bio-energy conversion. In 2021, she was awarded the Protein Society Anfinsen Award.
Alexandra Ros is a German analytical chemist who is a professor in both the School of Molecular Sciences and Center for Applied Structural Discovery at The Biodesign Institute, Arizona State University. Her research considers microfluidic platforms and their use in analysis. She was awarded the 2020 Advancing Electrokinetic Science Electrophoresis Society Mid-Career Achievement Award.
