4IV8

Crystal structure of N-methyl transferase from Plasmodium knowlesi complexed with S-adenosyl methionine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2012-02-15
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	P 21 21 2
Unit cell lengths	169.710, 96.760, 38.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.700 - 1.900
R-factor	0.2347
Rwork	0.233
R-free	0.27080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uj7
RMSD bond length	0.007
RMSD bond angle	1.147
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	20.000	1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.089	0.048	0.748
Number of reflections	51018	620	3679
<I/σ(I)>	12.81	28.73	2.56
Completeness [%]	99.8	89.7	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	282	Protein solution was at 15 mg/mL containing 20 mM Tris, 100 mM NaCl, 2 mM EDTA and 5 mM bME, 5 mM SAM. Mother liqueur contained 0.1 M Na-acetate (pH 5.0) and 20% PEG 3.350. Cryoprotectant was 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 282K