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3Q87

Structure of E. cuniculi Mtq2-Trm112 complex responible for the methylation of eRF1 translation termination factor

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSOLEIL BEAMLINE PROXIMA 1
Synchrotron siteSOLEIL
BeamlinePROXIMA 1
Temperature [K]100
Detector technologyCCD
Collection date2008-04-20
DetectorADSC QUANTUM 315r
Wavelength(s)1.214
Spacegroup nameP 21 21 21
Unit cell lengths42.115, 74.316, 96.754
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution48.377 - 1.997
R-factor0.2051
Rwork0.202
R-free0.25580
Structure solution methodSAD
RMSD bond length0.007
RMSD bond angle1.106
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwareSHARP
Refinement softwarePHENIX ((phenix.refine))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.220
High resolution limit [Å]1.9972.000
Number of reflections33750
<I/σ(I)>8.32
Completeness [%]97.996.9
Redundancy2.42.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION7.531020% PEG4000, 10% isopropanol, 100mM Hepes, pH 7.5, VAPOR DIFFUSION, temperature 310K

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