Knowledge of protein crystal perfection in theory and practice is reviewed. X-ray methods of assessing perfection such as mosaicity, topography and reciprocal-space mapping are described. X-ray diffraction physics applications of protein crystals such as in Laue geometry, the large-angle oscillation technique and forming polychromatic profiles across diffraction spots are covered. Cryo- and roo...

The structural information and functional insight obtained from X-ray crystallography can be enhanced by the use of complementary spectroscopies. Here the information that can be obtained from spectroscopic methods commonly used in conjunction with X-ray crystallography and best-practice single-crystal UV-Vis absorption data collection are briefly reviewed. Using data collected with the in situ...

X-ray crystallography is currently by far the most successful technique for determining the structures of biological macromolecules, their complexes and assemblies to high-resolution (better than 3.5 Å). These structures have been proven to assist the rational design of new drug-like molecules and they are invaluable in helping us to understand life at the atomic level. Nowadays, X-ray crystall...

Undulator radiation is the X-ray source of choice for modern macromolecular crystallography beamlines. Here, the basic properties of undulator sources are described and it is indicated why they make such good X-ray sources for macromolecular crystallography. Collection of excellent data from these beamlines is not always straightforward; therefore, a number of rules are postulated for undulator...

www.sciencemag.org SCIENCE VOL 343 7 MARCH 2014 COVER Precession image reconstructed from x-ray diffraction data collected from a benzene single crystal. For the past 100 years, x-ray crystallography has been a key tool for determining the structures of ever more complex chemical and biochemical systems. See the special section beginning on page 1091 and at www.sciencemag.org/special/crystallog...

We demonstrate that the soft X-ray diffraction pattern from a micron-size noncrystalline specimen can be recorded and inverted to form a high-resolution image. The phase problem is overcome by oversampling the diffraction pattern. The image is obtained using an iterative algorithm. The technique provides a method for X-ray microscopy requiring no highresolution X-ray optical elements or detecto...

A summary is given of the achievements and opportunities which resulted from the first use of an X-ray laser for serial crystallography and related methods in 2009.

Using the three-dimensional structure of biological macromolecules to infer how they function is one of the most important fields of modern biology. The availability of atomic resolution structures provides a deep and unique understanding of protein function, and helps to unravel the inner workings of the living cell. To date, 86% of the Protein Data Bank (rcsb-PDB) entries are macromolecular s...

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The intensities of a sufficient number of X-ray diffraction maxima determine the structure of a crystal, that is, the positions of the atoms in the unit cell of the crystal. The available intensities usually exceed the number of parameters needed to describe the structure. From these intensities a set of numbers jEHj can be derived, one corresponding to each intensity. However, the elucidation ...