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3HNA

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and mono-Methylated H3K9 Peptide

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-ID
Synchrotron siteAPS
Beamline19-ID
Temperature [K]100
Detector technologyCCD
Collection date2007-01-01
DetectorADSC QUANTUM 315
Wavelength(s)1
Spacegroup nameP 21 21 21
Unit cell lengths83.526, 83.372, 95.130
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution62.750 - 1.500
R-factor0.16738
Rwork0.166
R-free0.19273
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2rfi
RMSD bond length0.009
RMSD bond angle1.285
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 Overall
Low resolution limit [Å]100.000
High resolution limit [Å]1.500
Rmerge0.070
Number of reflections101405
<I/σ(I)>12
Completeness [%]96.5
Redundancy5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP630020%PEG3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K

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