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The amidase domain of the allophanate hydrolase AtzF from Pseudomonas sp. strain ADP has been crystallized and preliminary X-ray diffraction data have been collected.

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The rich history of crystallization and how that history influences current practices is described. The tremendous impact of crystallization screens on the field is discussed.

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As technology advances, the crystal volume that can be used to collect useful X-ray diffraction data decreases. The technologies available to detect and study growing crystals beyond the optical resolution limit and methods to successfully place the crystal into the X-ray beam are discussed.

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The PDB is looked at to find data to answer the question `How well do our current screens cover crystallization space?' and to try to find answers to the more general question about the most efficient strategy to employ in a crystallization campaign.
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