2ZQ8

Improvement of crystal quality by surface mutations of beta-lactamase Toho-1

(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 379-382

• PubMed: 19342785 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309109008240
• Primary Citation of Related Structures:  
  2ZQ8


• 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.

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Organizational Affiliation: 

RIKEN SPring-8 Center, Harima Institute, Kouto, Sayo, Hyogo 679-5148, Japan. t.shimamura@mfour.med.kyoto-u.ac.jp