Crystallographic data for the beta-lactamase from Enterobacter cloacae P99

Area of Science:

• Biochemistry
• Structural Biology
• Crystallography

Background:

• Beta-lactamase enzymes are crucial in bacterial resistance to antibiotics.
• Enterobacter cloacae P99 produces a beta-lactamase enzyme relevant to antibiotic resistance studies.

Purpose of the Study:

• To determine the crystal structure of beta-lactamase from Enterobacter cloacae P99.
• To provide insights into the enzyme's molecular architecture for potential drug development.

Main Methods:

• Crystallization of the beta-lactamase enzyme using polyethylene glycol solution.
• X-ray diffraction analysis of the resulting orthorhombic crystals.

Main Results:

• The beta-lactamase crystallized under specific conditions (pH 7, polyethylene glycol).
• Orthorhombic crystals were identified with space group P2(1)2(1)2.
• Unit cell dimensions were determined as a = 77.4 A, b = 69.4 A, and c = 63.4 A.
• One molecule of beta-lactamase (molecular weight 39,000) was found in the asymmetric unit.

Conclusions:

• The successful crystallization and X-ray analysis provide a structural basis for understanding Enterobacter cloacae P99 beta-lactamase.
• This structural data is vital for designing novel inhibitors to combat antibiotic resistance.