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Crystallization and preliminary X-ray analysis of the subclass B3 metallo-?-lactamase SMB-1 that confers carbapenem resistance.


ABSTRACT: The carbapenem-hydrolyzing subclass B3 metallo-?-lactamase SMB-1 was expressed in Escherichia coli and purified. Diffraction data were collected from two types of SMB-1 crystals that were obtained under different conditions. One crystal (SMB-1a) belonged to the trigonal space group P3(1) with unit-cell parameters a = b = 67.83, c = 48.67 Å, while the other crystal (SMB-1b) also belonged to space group P3(1) but with unit-cell parameters a = b = 67.25, c = 46.83 Å. Both crystals contained one molecule per asymmetric unit. Initial phases were determined by molecular replacement; further refinement and model building are in progress.

SUBMITTER: Wachino J 

PROVIDER: S-EPMC3310548 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the subclass B3 metallo-β-lactamase SMB-1 that confers carbapenem resistance.

Wachino Jun-ichi J   Yamaguchi Yoshihiro Y   Mori Shigetarou S   Yamagata Yuriko Y   Arakawa Yoshichika Y   Shibayama Keigo K  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120223 Pt 3


The carbapenem-hydrolyzing subclass B3 metallo-β-lactamase SMB-1 was expressed in Escherichia coli and purified. Diffraction data were collected from two types of SMB-1 crystals that were obtained under different conditions. One crystal (SMB-1a) belonged to the trigonal space group P3(1) with unit-cell parameters a = b = 67.83, c = 48.67 Å, while the other crystal (SMB-1b) also belonged to space group P3(1) but with unit-cell parameters a = b = 67.25, c = 46.83 Å. Both crystals contained one mol  ...[more]

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