Crystallization of recA protein from Proteus mirabilis

Area of Science:

• Structural biology
• Crystallography
• Molecular biology

Background:

• The recA protein plays a crucial role in DNA repair and recombination.
• Proteus mirabilis recA protein is homologous to Escherichia coli recA protein, suggesting conserved functions.

Purpose of the Study:

• To determine the crystal structure of the recA protein from Proteus mirabilis.
• To characterize the structural properties of Proteus mirabilis recA protein.

Main Methods:

• Crystallization of the recA protein from Proteus mirabilis.
• X-ray diffraction analysis to determine unit cell dimensions and space group.
• Analysis of the asymmetric unit to determine the number and molecular weight of subunits.

Main Results:

• Proteus mirabilis recA protein forms crystals in the orthorhombic space group P2(1)2(1)2(1).
• The asymmetric unit contains two subunits, each with a molecular weight of 38,000.
• Unit cell dimensions were determined as a = 57.5 A, b = 127.0 A, and c = 157.0 A.

Conclusions:

• The structural data provides a foundation for understanding the mechanism of recA protein function.
• Comparison with Escherichia coli recA protein may reveal conserved and unique structural features.