Crystallization and preliminary diffraction studies of a recombinant major urinary protein.
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 A, and beta = 93.24 degrees. The crystals diffract to beyond 1.4 A resolution at a synchrotron beamline.
Kuser
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P
Laboratório Nacional de Luz Síncrotron, Caixa Postal 6192, 13083-970 Campinas, São Paulo, Brazil. pkuser@lnls.br
Krauchenco
S
S
Fangel
A
A
Polikarpov
I
I
D000510:Alpha-Globulins / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D011487:Protein Conformation; D011506:Proteins; D011994:Recombinant Proteins / Q000737:chemistry
D000510:Alpha-Globulins; D011506:Proteins; D011994:Recombinant Proteins; C035737:major urinary proteins