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The crystal structure of NleC is reported at 1.55 Å resolution. In conjunction with biochemical analyses, the structure reveals that NleC is a member of the zincin zinc protease family and that the configuration of the NleC active site resembles that of the metzincin clan of metallopeptidases.

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The crystal structure of NleC is reported at 1.55 Å resolution. In conjunction with biochemical analyses, the structure reveals that NleC is a member of the zincin zinc protease family and that the configuration of the NleC active site resembles that of the metzincin clan of metallopeptidases.

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In this study, crystal structures of the E. coli Mre11 homologue SbcD and its Mn2+ complex are reported and an ssDNA-binding model is proposed for SbcD that differs from those of other Mre11 proteins, providing insight into the catalytic mechanism of the repair of DNA double-strand breaks by the Mre11 complex.

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A novel and simple protein crystallization method called the cross-diffusion microbatch method is presented. This method can dramatically increase the number of crystallization conditions and is a potentially useful technique in practical protein crystallization screening.

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The crystal structures of a first fungal glycoside hydrolase family 5 β-mannosidase from Rhizomucor miehei (RmMan5B) and of its inactive E202A mutant in complex with mannobiose, mannotriose and mannosyl-fructose are presented. Structural analyses reveal the structural basis of substrates binding.
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