1OR8

Structure of the Predominant protein arginine methyltransferase PRMT1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-05-18
Detector	CUSTOM-MADE
Wavelength(s)	1.1
Spacegroup name	P 41 2 2
Unit cell lengths	86.500, 86.500, 142.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.650 - 2.350
Rwork	0.195
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f3l
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.390
High resolution limit [Å]	2.350	2.350
Rmerge	0.037	0.195
Number of reflections	22428
<I/σ(I)>	20.7	3.2
Completeness [%]	96.3	61.1
Redundancy	3.455

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	4.7	289	ammonium phosphate, pH 4.7, VAPOR DIFFUSION, temperature 289K