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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 be...

Topics

Amino Acid Sequence
Binding Sites
Crystallization
Crystallography, X-Ray
Enzyme Stability
Hordeum
Hydrogen Bonding
Maltose
Models, Molecular
Molecular Sequence Data
Mutation
Plant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Secondary

Sequence Alignment

Temperature

beta-Amylase

Source

Identifiers

PMID: 9918723
DOI: 10.1006/jmbi.1998.2379

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9918723-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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