Here, we present the 2.5 Å structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 Å structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of ...

A mutant population of catalase I from Bacillus stearothermophilus prepared by this method has a diversity in thermostability and enzyme activity equal to that obtained after random point mutagenesis.

The biologic indicators are filter paper strips impregnated with spores of Geobacillus stearothermophilus and Bacillus atrophaeus enclosed in a glassine envelope. Throughout our 19 years of operation, ...