6CU5

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

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	2018-03-01
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	43.200, 101.450, 80.680
Unit cell angles	90.00, 100.10, 90.00

Refinement procedure

Resolution	42.751 - 2.700
R-factor	0.196
Rwork	0.188
R-free	0.26580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6cu3
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]	42.751	42.751	2.770
High resolution limit [Å]	2.700	12.070	2.700
Rmerge	0.117	0.058	0.561
Rmeas	0.134	0.067	0.640
Total number of observations	80274
Number of reflections	18861	224	1356
<I/σ(I)>	9.41	22.11	2.79
Completeness [%]	99.9	97.4	100
Redundancy	4.256	3.714	4.305
CC(1/2)	0.995	0.995	0.885

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 ProPlex screen condition F12 (1.5 M ammonium sulfate, 0.1 M sodium HEPES, pH 7.0), cryoprotectant: 20% ethylene glycol, crystal tracking ID 297887f12, unique puck ID bsj2-10