Lecture

X-ray Crystallography and SwissFEL

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In course

PHYS-468: Physics of life

Life has emerged on our planet from physical principles such as molecular self-organization, thermodynamics, stochastics and iterative refinement. This course will introduce the physical methods to study life and will discuss the quantitative and physical ...

Description

This lecture covers X-ray crystallography, protein structures, and the SwissFEL facility. It explains the process of determining protein structures using X-ray diffraction, the functioning of synchrotrons, and the advanced capabilities of SwissFEL in generating intense X-ray light for various research fields.

Instructor

Henning Paul-Julius Stahlberg

Mission We use high-resolution cryo-electron microscopy to study neurodegeneration and other protein systems. We also develop novel imaging technology in the areas of electron microscopy hardware and applications, sample preparation, data collection schemes, and data analysis software systems. The Stahlberg group is supported by the University of Lausanne, Faculty of Medicine and Biology, and by the EPFL, Faculty of Basic Sciences, Physics Institute. The LBEM is a research laboratory of both UNIL and EPFL.

Official source

Related concepts (26)

Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.

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.

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.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

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