2008Crystallography ReportsRequires access

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

Open publisher page 2 citations

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.

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 2 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Crystallization, Protein crystallization, Crystallography, Diffraction, X-ray crystallography, Resolution (logic), Crystal (programming language), Molecule

Related papers

Back to paper searchBrowse research topicsOriginal source
Crystallization and preliminary X-ray diffraction study of the protealysin precursor belonging to the peptidase family M4 — Research Paper | ScholarLens