Volume 55, Issue 7 pp. 1340-1341

Crystallization and preliminary diffraction studies of a recombinant major urinary protein

P. Kuser

P. Kuser

Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, 13083–970 Campinas, São Paulo, Brazil

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S. Krauchenco

S. Krauchenco

Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, 13083–970 Campinas, São Paulo, Brazil

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A. Fangel

A. Fangel

Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, 13083–970 Campinas, São Paulo, Brazil

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I. Polikarpov

I. Polikarpov

Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, 13083–970 Campinas, São Paulo, Brazil

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First published: 27 September 2007

Abstract

A monoclinic crystal form of a recombinant major urinary protein, (MUP) from mouse, has been obtained. MUP is a member of the lipocalin family whose biological function relates to olfaction and sexual communication. Crystals were grown by the vapour-diffusion technique against a mother liquor containing CdCl2. Crystals belong to the monoclinic space group P21 with the cell parameters a = 37.14, b = 55.79, c = 37.67 Å, and β = 93.24°. The crystals diffract to beyond 1.4 Å resolution at a synchrotron beamline.

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