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4Q4G

Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyCCD
Collection date2011-03-03
DetectorMARMOSAIC 225 mm CCD
Wavelength(s)0.9343
Spacegroup nameP 21 21 21
Unit cell lengths36.757, 65.505, 67.978
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.540 - 0.970
R-factor0.12627
Rwork0.126
R-free0.17462
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.028
RMSD bond angle2.174
Refinement softwareREFMAC (5.5.0110)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.000
High resolution limit [Å]0.9700.970
Number of reflections97211
Completeness [%]99.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.62935 and 8 mg mL-1 protein concentration, respectively, and 8% (v/v) 2-Propanol, 16% (w/v) PEG4000 in 60 mM Sodium citrate trihydrate buffer, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

220113

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