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2RFI

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and dimethylated H3K9 peptide

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 17-ID
Synchrotron siteAPS
Beamline17-ID
Temperature [K]100
Detector technologyCCD
Collection date2006-12-10
DetectorADSC QUANTUM 315
Wavelength(s)1.00000
Spacegroup nameP 21 21 21
Unit cell lengths84.593, 85.627, 95.670
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution42.800 - 1.590
R-factor0.19403
Rwork0.193
R-free0.22014
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2igq
RMSD bond length0.009
RMSD bond angle1.171
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 Overall
Low resolution limit [Å]42.800
High resolution limit [Å]1.590
Rmerge0.080
Number of reflections89676
<I/σ(I)>10.8
Completeness [%]96.5
Redundancy7.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP930016% PEG 4000, 10% Isopropanol, 0.1M Bicine pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K

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