TY - JOUR
T1 - Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution
AU - Bolognesi, Martino
AU - Coda, Alessandro
AU - Gatti, Giuseppina
AU - Ascenzi, Paolo
AU - Brunori, Maurizio
PY - 1985/5/5
Y1 - 1985/5/5
N2 - 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.
AB - 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.
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U2 - 10.1016/0022-2836(85)90285-2
DO - 10.1016/0022-2836(85)90285-2
M3 - Article
C2 - 4009720
AN - SCOPUS:0022419222
VL - 183
SP - 113
EP - 115
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -