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surface identified by NMR was flat and included a strip of three solvent-exposed Trp residues flanked by acidic residues. The overall structure of the AD2 was a TIM-barrel fold, which is a common fold in family 18 chitinases. The active site of the AD2 was in the groovelike cleft and was open to the solvent due to the lack of an additional small domain, which is observed in other family 18 chitinases.

Successful expression of archaeal STT3/AglB membrane protein inE.colicells