Crystallography in Biology

X-ray crystallography is the primary method for determining the molecular conformations of biological macromolecules, particularly protein and nucleic acids such as DNA and RNA. In fact, the double-helical structure of DNA was deduced from crystallographic data. The first crystal structure of a macromolecule was solved in 1958, a three-dimensional model of the myoglobin molecule obtained by X-ray analysis. The Protein Data Bank (PDB) is a freely accessible repository for the structures of proteins and other biological macromolecules. Computer programs such as RasMol or Pymol can be used to visualize biological molecular structures. Neutron crystallography is often used to help refine structures obtained by X-ray methods or to solve a specific bond; the methods are often viewed as complementary, as X-rays are sensitive to electron positions and scatter most strongly off heavy atoms, while neutrons are sensitive to nucleus positions and scatter strongly even off many light isotopes, including hydrogen and deuterium. Electron crystallography has been used to determine some protein structures, most notably membrane proteins and viral capsids.

  • X-ray crystallography
  • Neutron crystallography
  • Electron crystallography
  • Membrane Proteins Crystallography
  • Macromolecular Complexes and Assemblies
  • New tools and methods in structural biology
  • RasMol and Pymol
  • Structural plasticity of proteins
  • Hot Structures in Biology
  • Structural biology of signalling pathways
  • Macromolecular Complexes: Proteins/DNA/RNA

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