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1X2G

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL44XU
Synchrotron siteSPring-8
BeamlineBL44XU
Temperature [K]100
Detector technologyCCD
Collection date2003-05-31
DetectorBruker DIP-6040
Wavelength(s)0.9000
Spacegroup nameC 2 2 21
Unit cell lengths82.000, 112.800, 289.400
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution43.600 - 2.400
R-factor0.1742
Rwork0.171
R-free0.23337
Structure solution methodSAD
RMSD bond length0.021
RMSD bond angle1.830
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.490
High resolution limit [Å]2.4002.400
Rmerge0.0590.297
Number of reflections52725
<I/σ(I)>182.92
Completeness [%]99.499.7
Redundancy5.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5293ethylene glycol, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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