Year: 2000
Type: conference-abstract
Abstract: Crystals of B. lentus subtilisin, when cryo-cooled diffract to 0.85 Å resolution or better, which has been sufficient to resolve a special hydrogen bond within the catalytic triad at pH 5.9 (1) We have collected data from crystals at pH 5.0 and 8.6 where the enzyme is inactive or fully active.These data sets extend to a resolution of 0.85 and 0.76 Å, respectively.Both data sets in the outermost shell; are > 94% complete and have I/σ(I) ≥ 1.9.The aim of this work is to determine what changes may occur within the catalytic triad under conditions were the enzyme is inactive, partially and fully active.Preliminary difference electron density maps suggest that some subtle rearrangements do occur and refinement is underway.
Authors: R. Bott, G. Ganshaw, M. Soltis, P. Kuhn, M. Knapp
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2059516610