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3Q35

Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-B
Synchrotron siteAPS
Beamline23-ID-B
Temperature [K]100
Detector technologyCCD
Collection date2008-12-14
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.988
Spacegroup nameP 21 21 2
Unit cell lengths98.085, 119.001, 80.292
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution48.010 - 3.300
R-factor0.2091
Rwork0.207
R-free0.24800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3q33
RMSD bond length0.011
RMSD bond angle1.309
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwarePHENIX (1.6.4_486)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0003.420
High resolution limit [Å]3.3003.300
Number of reflections15302
<I/σ(I)>16.53.6
Completeness [%]99.797.2
Redundancy7.16.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.529810.0% (v/v) PEG8000; 8% (v/v) ethylene glycol; 100 mM Hepes, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.5

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