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3R0Q

A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU MICROMAX-007 HF
Temperature [K]298
Detector technologyIMAGE PLATE
Collection date2009-10-10
DetectorRIGAKU RAXIS IV++
Wavelength(s)1.5418
Spacegroup nameP 1 21 1
Unit cell lengths80.552, 86.691, 114.735
Unit cell angles90.00, 89.97, 90.00
Refinement procedure
Resolution32.970 - 2.610
R-factor0.1846
Rwork0.182
R-free0.22360
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.166
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHENIX
Refinement softwarePHENIX ((phenix.refine: 1.6.4_486))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]32.9702.670
High resolution limit [Å]2.6102.610
Number of reflections46744
<I/σ(I)>2.3
Completeness [%]96.691
Redundancy2.92.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.62950.1M Tris-HCl, 2.3M Na2HPO4, 0.1M arginine, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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