Autor: |
Fehlhammer, H., Schiffer, M., Epp, O., Colman, P., Lattman, E., Schwager, P., Steigemann, W., Schramm, H. |
Zdroj: |
Biophysics of Structure & Mechanism; 1975, Vol. 1 Issue 2, p139-146, 8p |
Abstrakt: |
The structure of a χ-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 å. 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. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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