Crystal structure of ferric Aplysia limacina myoglobin at 2 X 0 A resolution.

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.

journal_name

J Mol Biol

authors

Bolognesi M,Coda A,Gatti G,Ascenzi P,Brunori M

doi

10.1016/0022-2836(85)90285-2

subject

Has Abstract

pub_date

1985-05-05 00:00:00

pages

113-5

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(85)90285-2

journal_volume

183

pub_type

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