Download PDF by Jan Drenth: Principles of Protein X-ray Crystallography

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Extra resources for Principles of Protein X-ray Crystallography

Example text

6. Final check . Mount the screen and the radiation filter or monochromator. 20. (a) For simplicity the Ewald sphere is rotated instead of the reciprocal lattice. The vertical line in the center is the rotation axis. In its rotation around the axis the Ewald sphere never passes through the reciprocal lattice regions I-IV. " (b) Here the reciprocal lattice is in a skew position. In this example the reciprocal lattice has three perpendicular axes and, contrary to the situation in (a) , all reflections within one octant formed by the three reciprocal lattice axes can be measured .

Both instruments are push-button operated but require some maintenance: 1. a sealed tube must be replaced if the filament burns out and 2. a rotating anode tube occasionally needs a new filament (cathode) and new seals. Particle accelerators as synchrotrons and storage rings are the most powerful X-ray sources, but they are so complicated technically that the X-ray crystallographer is just a user at the front end. Because protein molecules are very large, their crystals diffract X-ray beams much less than do crystals of small molecules.

3. Schematic representation of the atomic energy levels and transitions causing characteristic X-ray wavelengths. The sharp peaks in the spectrum are due to electron transitions between inner orbitals in the atoms of the anode material. The high energy electrons reaching the anode shoot electrons out of low lying orbitals in the anode atoms. Electrons from higher orbitals occupy the empty positions and the energy released in this process is emitted as X-ray radiation of specific wavelength: Ka radiation if it comes from a transition from the L-shell to the K-shell and KI3 for a transition from the M- to the K-shell.

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