Abstract
In Chapter 1 you learned how crystals of a protein can be grown and you observed a diffraction pattern. The crystalline form of a protein is required to determine the protein’s structure by X-ray diffraction, but equally necessary are the tools for recording the diffraction pattern. These will be described in this chapter on hardware. The various X-ray sources and their special properties are discussed, followed by a description of cameras and detectors for quantitative and qualitative X-ray data collection.
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References
Wilhelm Conrad Roentgen, 1845–1925, discovered X-rays on November 8, 1895 in Würzburg, Germany.
Max von Laue, 1879–1960, German physicist, developed the theory of X-ray diffraction by a three-dimensional lattice.
Brilliance is defined as number of photons/sec/mrad2/mm2/0.1% relative bandwidth.
Background scattering is mainly caused by the air through which the X-ray beam passes from the collimator to the beamstop. If the airpath is long and absorption serious, it can appreciably be reduced if a cone filled with helium is put between the crystal and the plate.
This instrument is discussed in detail in Arndt and Wonacott (1977).
A full circle is 2π radians.
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© 1999 Springer Science+Business Media New York
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Drenth, J. (1999). X-ray Sources and Detectors. In: Principles of Protein X-ray Crystallography. Springer Advanced Texts in Chemistry. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-3092-0_2
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DOI: https://doi.org/10.1007/978-1-4757-3092-0_2
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4757-3094-4
Online ISBN: 978-1-4757-3092-0
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