1ORI

Structure of the predominant protein arginine methyltransferase PRMT1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X26C
Synchrotron site	NSLS
Beamline	X26C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-03-31
Detector	ADSC QUANTUM 4
Wavelength(s)	1.1
Spacegroup name	P 41 2 2
Unit cell lengths	88.270, 88.270, 145.140
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.180 - 2.500
Rwork	0.199
R-free	0.26300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f3l
RMSD bond length	0.008
RMSD bond angle	1.300
Data reduction software	HKL-2000
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	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.100	0.213
Total number of observations	102483 *
Number of reflections	20200
<I/σ(I)>	19.2	6.7
Completeness [%]	98.6	96.2
Redundancy	5.07

Crystallization Conditions

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

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	Tris	100 (mM)	pH9.0
3	1	reservoir	ammonium phosphate monobasic	1.6 (M)	pH4.7