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A novel high-throughput in situ plate-screening procedure is used to assess the effect of dehydration on a membrane-associated protein. In this case the dehydration improved the diffraction quality of the crystal.

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The putative methyltransferase CmoA is involved in the nucleoside modification of transfer RNA. X-ray crystallography and mass spectrometry are used to show that it contains a novel SAM derivative, S-adenosyl-S-carboxymethyl-L-homocysteine, in which the donor methyl group is replaced by a carboxymethyl group.

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