Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution
Journal of Molecular BiologyPublished 1 May 1985
Martino Bolognesi, Alessandro Coda, Giuseppina Gatti, Paolo Ascenzi, Maurizio Brunori
Citations33
SJR quartileQ1
SJR score2.21
SNIP1.13
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TL;DR
The three-dimensional structure of ferric myoglobin from the mollusc Aplysia limacina has been refined at 2 X 0 A resolution and it conforms to the common eight-helices globin fold observed in other phyla.
Abstract
The three-dimensional structure of ferric myoglobin from the mollusc Aplysia limacina has been refined at 2 X 0 A resolution. The crystallographic R factor, calculated at this stage, is 0 X 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.
Keywords
Biochemistry, Genetics and Molecular Biology
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