3.2.1.B26	-	
3.2.1.B26	structures, at approximately 2 A resolution, of the enzyme in complex with both covalently (derived from 2-fluoro-glycosides) and noncovalently (hydroximolactam) bound inhibitors	
3.2.1.B26	the crystal structure is determined using multiple isomorphous replacement assisted by solvent flattening, histogram equalisation and non-crystallographic symmetry averaging, and refined at 2.6 A resolution. the enzyme crystallises as a tetramer with 222 point group symmetry, one dyad of which is crystallographic, with a dimer in the asymmetric unit. Analysis of the structure reveals two features which differ significantly from mesophile proteins: (1) an unusually large proportion of surface ion-pairs involved in networks that cross-link sequentially separate structures on the protein surface, and (2) an unusually large number of solvent molecules buried in hydrophilic cavities between sequentially separate structures in the protein core. These factors suggest a model for hyperthermostability via resilience rather than rigidity