1F3L

CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3

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	1999-05-01
Detector	BRANDEIS - B2
Wavelength(s)	0.93
Spacegroup name	P 43 21 2
Unit cell lengths	70.910, 70.910, 177.660
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.870 - 2.030
R-factor	0.209
Rwork	0.209
R-free	0.26200
RMSD bond length	0.008
RMSD bond angle	27.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000
High resolution limit [Å]	2.030 *
Rmerge	0.057 *	0.210 *
Number of reflections	27345 *	1659 *
Completeness [%]	90.9 *	56.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.3	289	PEG4000, AMMONIUM ACETATE, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 289K
1	unknown *	6.3	289	PEG4000, AMMONIUM ACETATE, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 289K
1	unknown *	6.3	289	PEG4000, AMMONIUM ACETATE, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 289K
1	unknown *	6.3	289	PEG4000, AMMONIUM ACETATE, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	Mes	100 (mM)
2	1	1	PEG4000	16.5-18 (%)
3	1	1	ammonium acetate	0.2 (M)