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New crystal form of β-lactoglobulin

Published online by Cambridge University Press:  01 June 2009

Thales L. Rocha ,
Sharon Brownlow ,
Keith N. Saddler ,
Linda A. Fothergill-Gilmore  and
Lindsay Sawyer
Thales L. Rocha
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Sharon Brownlow
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Keith N. Saddler
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Linda A. Fothergill-Gilmore
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Lindsay Sawyer
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
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Summary

The milk whey protein β-lactoglobulin has been isolated from ovine milk, purified and crystallized in a form suitable for X-ray crystallography. The crystals, which diffract to 1·9 Å resolution, belong to the trigonal space group P3121 with unit cell lengths a = b = 99·8 Å, c = 67·7 Å and unique angle γ = 120·0°. Although there have been many crystal forms reported for bovine β-lactoglobulin, none has been reported with these unit cell parameters. A preliminary native data set has been collected and a molecular replacement solution obtained, using the structure of dimeric bovine β-lactoglobulin as the search model. The importance of the ovine structure in relation to that of the bovine is discussed.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 4 , November 1996 , pp. 575 - 584
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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References

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