Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution

Martino Bolognesi, Alessandro Coda, Giuseppina Gatti, Paolo Ascenzi, Maurizio Brunori

Research output: Contribution to journalArticlepeer-review

Abstract

The three-dimensional structure of ferric myoglobin from the mollusc Aplysia limacina has been refined at 2.0 Å resolution. The crystallographic R factor, calculated at this stage, is 0.194. Despite its high content of apolar residues (both aromatic and aliphatic), Aplysia limacina myoglobin, which contains only one histidine residue (at the proximal position), has a structure that conforms to the common eight-helices globin fold observed in other phyla.

Original languageEnglish
Pages (from-to)113-115
Number of pages3
JournalJournal of Molecular Biology
Volume183
Issue number1
DOIs
Publication statusPublished - May 5 1985

ASJC Scopus subject areas

  • Virology

Fingerprint Dive into the research topics of 'Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution'. Together they form a unique fingerprint.

Cite this