5LFU

Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P14 (MX2)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2013-12-15
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.97553
Spacegroup name	P 65 2 2
Unit cell lengths	101.237, 101.237, 687.477
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	114.579 - 4.300
R-factor	0.2859
Rwork	0.285
R-free	0.29550
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1url 4frw 1cs6 3p3y 2yd6
RMSD bond length	0.008
RMSD bond angle	1.331
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	114.620	4.810
High resolution limit [Å]	4.300	4.300
Rmerge	0.115	3.937
Number of reflections	15430
<I/σ(I)>	15.6	1.3
Completeness [%]	100.0	100
Redundancy	35.7	36.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	Crystals were grown from protein that was modified by reductive lysine methylation. Protein was concentrated to 8.4 mg/mL, which was mixed 1:1 with reservoir solution. Crystals grew in a condition containing 200 mM NaOAc and 20 % PEG3350 (w/v).