J Mol Biol. 1991 Apr 20;218(4):699-701.

Crystallization of and preliminary X-ray data for the mouse major urinary protein and rat alpha-2u globulin.

Böcskei Z, Findlay JB, North AC, Phillips SE, Somers WS, Wright CE, Lionetti C, Tirindelli R, Cavaggioni A.

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Department of Biochemistry and Molecular Biology, University of Leeds, U.K.

Abstract

Crystals of the mouse major urinary protein (MUP) and rat alpha-2u globulin (AMG) have been grown from solutions of polyethylene glycol 3350 and CdCl2, respectively. The crystals differ both in their morphologies and space groups but have very similar unit cell sizes. AMG crystallized in P2(1) (a = 56.6 A, b = 103.8 A, c = 62.7 A, beta = 95.1 degrees) with four subunits/asymmetric unit, while MUP gave crystals in P4(1)2(1)2 or P4(3)2(1)2 (a = 57.3 A, c = 109.9 A) with one subunit/asymmetric unit. Both crystal forms diffract beyond 2.8 A resolution.

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Structures reported by this article

Pheromone Binding To Two Rodent Urinary Proteins Revealed By X-Ray Crystallography

PDB: 1MUP

Source: Mus musculus

Method: X-Ray Diffraction

Resolution: 2.4 Å

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