Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product.

doi:10.1006/jmbi.1994.1688

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product.

Journal of molecular biology - 11 Nov 1994

Hadfield A T, Harvey D J, Archer D B, MacKenzie D A, Jeenes D J, Radford S E, Lowe G, Dobson C M, Johnson L N

Abstract excerpt

The crystal structure of a mutant hen egg white lysozyme, in which the key catalytic residue aspartic acid 52 has been changed to a serine residue (D52S HEWL), has been determined and refined to a crystallographic R value of 0.173 for all data F > 0 between 8 and 1.9 A resolution. The D52S HEWL s...

Topics

Animals
Carbohydrate Sequence
Chickens
Crystallography, X-Ray
Egg White
Hydrogen Bonding
Mass Spectrometry
Molecular Sequence Data
Molecular Structure
Muramidase
Mutation
Oligosaccharides

Source

Open in PubMed

Identifiers

PMID: 7966306
DOI: 10.1006/jmbi.1994.1688

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7966306-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics