Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution

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

doi:10.1016/0022-2836(85)90285-2

Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution

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

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article

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 language	English
Pages (from-to)	113-115
Number of pages	3
Journal	Journal of Molecular Biology
Volume	183
Issue number	1
DOIs	https://doi.org/10.1016/0022-2836(85)90285-2
Publication status	Published - May 5 1985

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ASJC Scopus subject areas

Virology

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Bolognesi, M., Coda, A., Gatti, G., Ascenzi, P., & Brunori, M. (1985). Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution. Journal of Molecular Biology, 183(1), 113-115. https://doi.org/10.1016/0022-2836(85)90285-2

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10.1016/0022-2836(85)90285-2