Article
The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution.
Journal of molecular biology - 22 Jan 1999
Mikami B, Yoon H J, Yoshigi N
Abstract excerpt
The three-dimensional structure of the sevenfold mutant of barley beta-amylase (BBA-7s) with increased thermostability was determined by X-ray crystallography. The enzyme was purified as a single component and crystallized by a hanging drop method in the presence of 14 % PEG 6000. The crystals belong to space group P43212 with cell dimensions a=b=72.11 A, c=250.51 A. The diffraction data up to 2.5 A were...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
