Abstract
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.
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Extract from Dissertation, München (1974).
on leave from the Division of Biological and Medical Research, Argonne National Laboratory, Argonne, Illinois 60439, USA.
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Fehlhammer, H., Schiffer, M., Epp, O. et al. The structure determination of the variable portion of the Bence-Jones protein Au. Biophys. Struct. Mechanism 1, 139–146 (1975). https://doi.org/10.1007/BF00539775
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DOI: https://doi.org/10.1007/BF00539775