The structure of a pi-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur J. Biochem. 45, 513 (1974). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 A. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones and of the internal residues is extremely similar to that found in Rei.
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| rdf:type | |
| rdfs:comment |
The structure of a pi-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur J. Biochem. 45, 513 (1974). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 A. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones and of the internal residues is extremely similar to that found in Rei.
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| skos:exactMatch | |
| uniprot:name |
Biophys. Struct. Mech.
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| uniprot:author |
Colman P.M.,
Epp O.,
Fehlhammer H.,
Lattman E.E.,
Schiffer M.,
Schramm H.J.,
Schwager P.,
Steigemann W.
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| uniprot:date |
1975
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| uniprot:pages |
139-146
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| uniprot:title |
The structure determination of the variable portion of the Bence-Jones protein Au.
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| uniprot:volume |
1
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