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All seven possible single-site lysine-to-serine mutations of ubiquitin were tested for crystallization behavior and were found to yield crystallization `hit rates' varying by two orders of magnitude. High-resolution structures of three mutants revealed that mutations can exert both promoting and permissive effects on crystallization.

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In the last three decades, membrane-protein crystallization has changed from overwhelmingly difficult to nearly routine. This review offers a snapshot of the current state of the art, focusing particularly on the role of detergents in this process.
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