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1P0Y

Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]95
Detector technologyIMAGE PLATE
Collection date2003-01-25
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameI 2 2 2
Unit cell lengths130.410, 153.190, 266.320
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 2.550
R-factor0.228
Rwork0.228
R-free0.26900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1mlv
RMSD bond length0.007
RMSD bond angle21.300

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS (1.1)
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.640
High resolution limit [Å]2.5502.550
Rmerge0.044

*

0.485

*

Number of reflections838297768

*

<I/σ(I)>30.22.45
Completeness [%]96.593.6
Redundancy4.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.825

*

0.95-1.10 M Sodium Acetate, 100 mM Methyllysine Acetate, 1 mM TCEP, 400 uM S-adenosylhomocysteine, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoirsodium acetate0.95-1.10 (M)
31reservoirAdoHcy4000 (nM)
41reservoirTCEP1 (mM)
51reservoirLys100 (mM)or MeLys, pH6.8

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PDB entries from 2024-08-28

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