Lecture

Macromolecular Crystallography: Techniques and Applications

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

Description

This lecture covers the techniques and applications of synchrotrons and x-ray free-electron lasers in macromolecular crystallography. The instructor explains the phase problem for large molecules, detailing approaches like multiple isomorphous replacement, multiwavelength anomalous dispersion, and single-wavelength anomalous diffraction. Various macromolecular crystallography approaches are discussed, including Multiple/Single Isomorphous Replacement, Multiwavelength Anomalous Dispersion, and Single-Wavelength Anomalous Diffraction. The lecture also explores trends in MX phasing techniques, such as MIR, SIR, and MAD. Practical examples like the COVID-19 main protease and Benzylpenicillin are used to illustrate the concepts.

Official source

Ontological neighbourhood

Earth science

Geology: Mineralogy

Related concepts (32)

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.

Phase problem

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. Light detectors, such as photographic plates or CCDs, measure only the intensity of the light that hits them.

Structural bioinformatics

Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds and local motifs, principles of molecular folding, evolution, binding interactions, and structure/function relationships, working both from experimentally solved structures and from computational models.

Crystallographic database

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 structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Related lectures (64)

X-ray Crystallography and SwissFEL

Delves into X-ray crystallography, protein structures, and the cutting-edge SwissFEL facility.

Protein Structure Determination: X-ray vs NMR

Explores protein structure determination using X-ray crystallography and NMR spectroscopy, covering historical significance, crystal formation, diffraction patterns, and challenges in crystallization.

Glass Transition: Polymer Properties

Explores glass and melting transitions in polymers, including characterization methods and specific polymer properties.

Protein Structure Determination

Explores protein structure determination through X-ray crystallography, NMR spectroscopy, and Cryo-EM, covering crystallization, diffraction patterns, and atomic models.

Crystal Structure Determination by 3D Electron Diffraction