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1H3I

Crystal structure of the Histone Methyltransferase SET7/9

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
DetectorADSC CCD
Wavelength(s)0.9794, 0.9394, 0.9800
Spacegroup nameP 21 21 21
Unit cell lengths66.090, 82.830, 116.150
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 2.100
R-factor0.212
Rwork0.210
R-free0.25800

*

Structure solution methodMAD
RMSD bond length0.010
RMSD bond angle1.500

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareREFMAC (5.0)
Data quality characteristics
 Overall
Low resolution limit [Å]30.000

*

High resolution limit [Å]2.100
Rmerge0.048

*

Number of reflections37053
Completeness [%]84.0

*

Redundancy3.1

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

7pH 7.00
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropTris50 (mM)pH7.0
31drop100 (mM)
41dropTCEP1 (mM)
51reservoirmagnesium formate0.2 (M)
61reservoirPEG335025 (%)

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PDB entries from 2024-12-25

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