5OFB

Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy mutation S87L

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	69.850, 124.680, 80.360
Unit cell angles	90.00, 97.73, 90.00

Refinement procedure

Resolution	79.630 - 2.020
R-factor	0.1994
Rwork	0.198
R-free	0.22764
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Wild-type human MORC2
RMSD bond length	0.015
RMSD bond angle	1.939
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]	79.629	79.629	2.053
High resolution limit [Å]	2.018	5.478	2.018
Rmerge	0.052	0.031	0.648
Rpim	0.042	0.025	0.529
Number of reflections	82175	4507	4331
<I/σ(I)>	13.5	28.9
Completeness [%]	91.9	98.9	96.7
Redundancy	3.8	3.8	3.7
CC(1/2)	0.999	0.998	0.800

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	0.1 M bicine/Trizma pH 8.5 10.2% PEG 4k 20.4% 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