6CU3

Crystal structure of a protein arginine N-methyltransferase from Naegleria fowleri

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2017-08-18
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 2
Unit cell lengths	249.630, 101.460, 105.890
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.997 - 2.500
R-factor	0.1908
Rwork	0.190
R-free	0.23270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3q7e
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.997	46.997	2.560
High resolution limit [Å]	2.500	11.180	2.500
Rmerge	0.077	0.023	0.558
Rmeas	0.085	0.026	0.616
Total number of observations	504864
Number of reflections	93675	1146	6834
<I/σ(I)>	16.18	40.07	3.11
Completeness [%]	99.9	96	100
Redundancy	5.39	4.524	5.485
CC(1/2)	0.999	0.999	0.887

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	291	5.5 mg/mL NafoA.01523.a.B1.PW37976 against JCSG+ screen condition A3 (0.2 M ammonium citrate, 25% PEG3350), cryoprotectant: 20% ethylene glycol, crystal tracking ID 286783a3, unique puck ID rmz3-7