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7EV6

Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with F-b20-Q

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL44XU
Synchrotron siteSPring-8
BeamlineBL44XU
Temperature [K]100
Detector technologyCCD
Collection date2011-06-11
DetectorBRUKER SMART 6500
Wavelength(s)1
Spacegroup nameP 6
Unit cell lengths115.826, 115.826, 136.256
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution19.850 - 2.100
R-factor0.156
Rwork0.154
R-free0.17800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)4fw9
RMSD bond length0.010
RMSD bond angle1.399
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.170
High resolution limit [Å]2.1002.100
Rmerge0.0570.891
Number of reflections5741248926
<I/σ(I)>29.82.3
Completeness [%]95.390.9
Redundancy6.55.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP4.629510% isopropanol, 100mM monosodium phosphate, 100mM sodium citrate

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