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4FWH

Crystal structure of the Lon-like protease MtaLonC in complex with MG262

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSRRC BEAMLINE BL13C1
Synchrotron siteNSRRC
BeamlineBL13C1
Temperature [K]100
Detector technologyCCD
Collection date2011-06-22
DetectorADSC QUANTUM 315r
Wavelength(s)1.0
Spacegroup nameP 6
Unit cell lengths115.995, 115.995, 136.124
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.190
R-factor0.17619
Rwork0.174
R-free0.22675
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4fw9
RMSD bond length0.025
RMSD bond angle2.366
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.6.0117)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.180
High resolution limit [Å]2.1002.100
Rmerge0.0910.852
Number of reflections59267
<I/σ(I)>40.14.4
Completeness [%]97.994.6
Redundancy10.29.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP4.629510% isopropanol, 200mM di-potassium phosphate, 100mM sodium citrate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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