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5ZRC

Structural insights into the catalysis mechanism of M. smegmatis antimutator protein MutT2

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyCCD
Collection date2014-12-31
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.8266
Spacegroup nameP 21 21 2
Unit cell lengths65.840, 59.870, 31.500
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution16.460 - 1.100
R-factor0.14364
Rwork0.142
R-free0.17247
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2rrk
RMSD bond length0.016
RMSD bond angle1.643
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwarePHASER
Refinement softwareREFMAC (5.8.0049)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]16.4601.160
High resolution limit [Å]1.1001.100
Rmerge0.0620.770
Number of reflections490976891
<I/σ(I)>163
Completeness [%]95.993.4
Redundancy4.84.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1MICROBATCH2920.1 M MES monohydrate pH 6.0, 20%(v/v) Jeffamine M-600 pH 7.0

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