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. 1975 Feb 19;1(2):139-46.
doi: 10.1007/BF00539775.

The structure determination of the variable portion of the Bence-Jones protein Au

H Fehlhammer, M Schiffer, O Epp, P M Colman, E E Lattman, P Schwager, W Steigemann, H J Schramm

The structure determination of the variable portion of the Bence-Jones protein Au

H Fehlhammer et al. Biophys Struct Mech. .

Abstract

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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References

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