8FT7

Crystal structure of SAH bound protein arginine N-methyltransferase 1 (PRMT1) from Naegleria fowleri

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-12-10
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.97856
Spacegroup name	I 21 21 21
Unit cell lengths	80.586, 147.886, 152.054
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.600 - 2.150
R-factor	0.1906
Rwork	0.189
R-free	0.22760
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	0.922
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.950	2.220
High resolution limit [Å]	2.150	2.150
Rmerge	0.058	1.485
Rmeas	0.060	1.539
Rpim	0.016	0.403
Total number of observations	680729	61863
Number of reflections	49721	4272
<I/σ(I)>	21.9	2.1
Completeness [%]	100.0
Redundancy	13.7	14.5
CC(1/2)	0.999	0.768

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291	Wizard Cryo H6: 30% PEG 200, 100mM Sodium Acetate pH 4.5, 100mM Sodium Chloride. NafoA.20639.a.A2.PW39094 at 8.5 mg/mL Tray: Steve 11/09/22 well D10, 24 hour soak in 5mM S-adenosylhomocysteine (SAH), Puck: PSL0710, Cryo: direct