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5KNK

Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii with catalytic residue substitution (E127A)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.2
Synchrotron siteALS
Beamline5.0.2
Temperature [K]80
Detector technologyCCD
Collection date2016-04-08
DetectorADSC QUANTUM 315r
Wavelength(s)1.0000
Spacegroup nameC 2 2 21
Unit cell lengths59.300, 145.470, 87.610
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution72.735 - 1.900
R-factor0.2265
Rwork0.225
R-free0.27120
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)5kn7
RMSD bond length0.007
RMSD bond angle1.100
Data reduction softwareiMOSFLM
Data scaling softwareAimless
Phasing softwarePHASER
Refinement softwarePHENIX (1.10_2155)
Data quality characteristics
 Overall
Low resolution limit [Å]72.740
High resolution limit [Å]1.900
Number of reflections30262
<I/σ(I)>7.95
Completeness [%]100.0
Redundancy1.9
CC(1/2)0.998
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.5293200 mM KBr 2.2 M (NH4)2SO4

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