Crystallization and preliminary X-ray diffraction study of the protealysin precursor belonging to the peptidase family M4
T. Yu. Gromova, Ilya V. Demidyuk, Sergey V. Kostrov, N. I. Sosfenov, V. R. Melik-Adamyan, Inna P. Kuranova
Abstract
T. Yu. Gromova, Ilya V. Demidyuk, Sergey V. Kostrov, N. I. Sosfenov, V. R. Melik-Adamyan, Inna P. Kuranova
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-dimensional structure of the protein molecule at atomic resolution.
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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-dimensional structure of the protein molecule at atomic resolution.
Key concepts: Crystallization, Protein crystallization, Crystallography, Diffraction, X-ray crystallography, Resolution (logic), Crystal (programming language), Molecule