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5UX9

The crystal structure of chloramphenicol acetyltransferase from Vibrio fischeri ES114

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyPIXEL
Collection date2017-02-08
DetectorDECTRIS PILATUS3 S 6M
Wavelength(s)0.97919
Spacegroup nameP 63
Unit cell lengths147.426, 147.426, 101.211
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution47.045 - 2.700
R-factor0.2018
Rwork0.200
R-free0.23970
Structure solution methodSAD
RMSD bond length0.003
RMSD bond angle0.568
Data reduction softwareHKL-3000
Data scaling softwareHKL-3000
Phasing softwareHKL-3000
Refinement softwarePHENIX ((1.11.1_2575))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.750
High resolution limit [Å]2.7002.700
Rmerge0.0550.779
Rpim0.0270.400
Number of reflections341581724
<I/σ(I)>21.62.5
Completeness [%]99.199.4
Redundancy4.24.1
CC(1/2)0.705
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.52890.2 M Magnesium Chloride, 0.1 M MES:NaOH, 10% (w/v) PEG4000

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