Crystallization of alcohol oxidase fromPichia pastoris. Secondary structure predictions indicate a domain with the eightfold β/α-barrel fold

Abstract
Alcohol oxidase fromPichia pastoris has been crystallized from polyethylene glycol 4000 solutions. The crystals are tetragonal, a=228 Å, c=456 Å space groupP41212. The crystals scatter only to about 6 Å resolution; their poor crystallinity may have some physiological function. Secondary structure predictions suggest that the C-terminal part of the molecule, residues 311–664, has the folding of an eightfold β/α-barrel (TIM barrel). This would indicate common ancestry with four other flavoenzymes: canavalin, glycolate oxidase, flavocytochrome b, and trimethylamine dehydrogenase.