2ZQ8

Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant

Summary for 2ZQ8

• Entry DOI: 10.2210/pdb2zq8/pdb
• Related: 2ZQ7 2ZQ9 2ZQA 2ZQC 2ZQD
• Descriptor: Beta-lactamase Toho-1, SULFATE ION (3 entities in total)
• Functional Keywords: extended-spectrum, esbl, beta-lactamase, toho-1, hydrolase, antibiotic resistance, plasmid
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 28656.10

Authors

Shimamura, T.,Nitanai, Y.,Uchiyama, T.,Ago, H.,Matsuzawa, H.,Miyano, M. (deposition date: 2008-08-07, release date: 2009-07-28, Last modification date: 2023-11-01)

Primary citation

Shimamura, T.,Nitanai, Y.,Uchiyama, T.,Matsuzawa, H.
Improvement of crystal quality by surface mutations of beta-lactamase Toho-1
Acta Crystallogr.,Sect.F, 65:379-382, 2009

PubMed Abstract: The beta-lactamase Toho-1 exhibits a strong tendency to form merohedrally twinned crystals. Here, the crystal quality of Toho-1 was improved by using surface modification to remove a sulfate ion involved in crystal packing. The surface-modified Toho-1 variant (R274N/R276N) was crystallized under similar conditions to those used for wild-type Toho-1. R274N/R276N did not form merohedrally twinned crystals. The crystals diffracted to a significantly higher resolution (approximately 0.97 A) than the wild-type crystals (1.65 A); they belonged to the same space group and had almost identical unit-cell parameters to those of wild-type Toho-1.

PubMed: 19342785
DOI: 10.1107/S1744309109008240

Experimental method

X-RAY DIFFRACTION (1.03 Å)