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. 1987 Mar 1;242(2):353–360. doi: 10.1042/bj2420353

Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme.

S G Smith, M Lewis, R Aschaffenburg, R E Fenna, I A Wilson, M Sundaralingam, D I Stuart, D C Phillips
PMCID: PMC1147712  PMID: 3593255

Abstract

The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.45 nm) resolution by the method of isomorphous replacement. The principal derivative was prepared by reducing a disulphide bridge in the crystals and inserting a mercury atom. Detailed comparison of the electron-density maps with corresponding maps of hen egg-white lysozyme shows that they are closely similar, with correlation coefficients of 0.57 and 0.44 at 6 A and 4.5 A resolution respectively. This result, in accordance with earlier predictions based upon comparisons of amino-acid sequences, provides further evidence that class C lysozymes and alpha-lactalbumins are homologous proteins and it is in keeping with the hypothesis that the alpha-lactalbumins evolved from a lysozyme precursor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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