5OFA

Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy mutation T424R

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-04-15
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.975999
Spacegroup name	P 1 21 1
Unit cell lengths	69.610, 125.730, 81.530
Unit cell angles	90.00, 97.91, 90.00

Refinement procedure

Resolution	80.750 - 2.570
R-factor	0.21275
Rwork	0.211
R-free	0.23938
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Wild-type human MORC2
RMSD bond length	0.014
RMSD bond angle	1.935
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	80.755	80.755	2.619
High resolution limit [Å]	2.574	6.986	2.574
Rmerge	0.046	0.031	0.599
Rpim	0.037	0.018	0.483
Number of reflections	43876	8051	8044
<I/σ(I)>	16.2	32.8	2.1
Completeness [%]	99.6	99.2	99.4
Redundancy	3.8	3.6	3.7
CC(1/2)	0.999	0.998	0.797

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	0.1 M bicine/Trizma pH 8.5 10.8% PEG 4k 21.6% glycerol 0.02 M each of the following: 1,6-hexanediol; 1-butanol; RS-1,2 propanediol; 2-propanol; 1,4-butanediol; 1,3-propanediol