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Crystal structures of S-adenosyl-L-homocysteine hydrolase from L. luteus in complex with adenosine, cordycepin and adenine are presented.

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The crystal structures of the far-red fluorescent proteins eqFP650 and eqFP670 have been solved at 1.8 and 1.6 Å resolution, respectively. This permitted identification of the structural elements responsible for the bathochromic shift in both considered far-red fluorescent proteins.

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A repetitive measurement of the same diffraction image allows to judge the performance of a data collection facility.

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The N-terminal domain of the PriB protein from the thermophilic bacterium T. tengcongensis (TtePriB) was expressed and its crystal structure has been solved at the atomic resolution of 1.09 Å by direct methods.
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