8DUR

Crystal structure of apo 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	2022-06-07
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.97856
Spacegroup name	I 21 21 21
Unit cell lengths	80.501, 147.708, 150.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.480 - 1.970
R-factor	0.1969
Rwork	0.196
R-free	0.22300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6cu3
Data reduction software	XDS
Data scaling software	Aimless (0.7.8)
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.420	47.420	2.020
High resolution limit [Å]	1.970	9.030	1.970
Rmerge	0.050	0.026	0.887
Rmeas	0.054	0.028	0.960
Rpim	0.020	0.011	0.365
Total number of observations	455633	4725	30175
Number of reflections	63443	738	4421
<I/σ(I)>	18.6	54.1	2.2
Completeness [%]	99.9	98.4	100
Redundancy	7.2	6.4	6.8
CC(1/2)	0.999	0.999	0.728

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291	Berkeley D8: 100mM MES pH 5.5, 100 mM Ammonium Citrate dibasic, 20% (w/v) PEG 3350, 5% (v/v) 2-propanol. NafoA.20639.a.A2.PW39094 at 8.5 mg/mL Tray: Original crystals from plate 12655, well D8 drop 1, reproduced these crystals in a Clover Jr. plate (Rigaku reagents), Puck: PSL1001, Cryo: 80% (v/v) crystallant + 20% (v/v) ethylene glycol