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9BGP

X-ray structure of the aminotransferase from Vibrio vulnificus responsible for the biosynthesis of 2,3-diacetamido-4-amino-2,3,4-trideoxy-arabinose in the presence of its internal aldimine

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSEALED TUBE
Source detailsBRUKER D8 QUEST
Temperature [K]100
Detector technologyPIXEL
Collection date2023-07-22
DetectorBruker PHOTON II
Wavelength(s)1.5418
Spacegroup nameP 1
Unit cell lengths53.110, 53.116, 70.322
Unit cell angles82.59, 82.56, 74.40
Refinement procedure
Resolution33.450 - 1.250
R-factor0.16848
Rwork0.167
R-free0.18813
Structure solution methodFOURIER SYNTHESIS
RMSD bond length0.007
RMSD bond angle1.520
Data reduction softwareSAINT
Data scaling softwareSADABS
Phasing softwarePHASER
Refinement softwareREFMAC (5.8.0405)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.350
High resolution limit [Å]1.2501.250
Number of reflections19939139859
<I/σ(I)>10.72.8
Completeness [%]98.695.6
Redundancy4.92.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP52938-12% (w/v) poly(ethylene glycol) 8000, 200 mM LiCl, and 100 mM Homo-PIPES (pH 5.0)

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