Crystallization and Preliminary X-Ray Diffraction Study
of the Protealysin Precursor Belonging
to the Peptidase Family M4

T. Yu. Gromova^{a, b}, I. V. Demidyuk^a, S. V. Kostrov^a, N. I. Sosfenov^c,
V. R. Melik-Adamyan^c, and I. P. Kuranova^c

^a Institute of Molecular Genetics, Russian Academy of Sciences, pl. Kurchatova 2, Moscow, 123182 Russia

e-mail: duk@img.ras.ru

^b Moscow State Academy of Fine Chemical Technology, pr. Vernadskogo 86, Moscow, 119571 Russia

e-mail: tgromova81@mail.ru

^c Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninski pr. 59, Moscow, 119333 Russia

e-mail: inna@ns.crys.ras.ru

Received December 26, 2007

Abstract—A protealysin precursor (the enzyme of the peptidase family M4) was crystallized for the first time.
The crystal-growth conditions were found, and single crystals of the protein with dimensions of 0.3–0.5 mm
were grown. The preliminary X-ray diffraction study of the enzyme was performed. The protealysin precursor
was shown to crystallize in two crystal modifications suitable for the X-ray diffraction study of the three-dimen-
sional structure of the protein molecule at atomic resolution.

PACS numbers: 87.15.nt

DOI: 10.1134/S1063774508050118

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