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

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 respec...

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Publication status:
Published

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Authors


Aschaffenburg, R More by this author
Wilson, IA More by this author
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Journal:
The Biochemical journal
Volume:
242
Issue:
2
Pages:
353-360
Publication date:
1987-03-05
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:36af9036-eb4f-4343-bb2b-a0aecae69230
Source identifiers:
5220
Local pid:
pubs:5220

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