6QGE

Galectin-3C in complex with a pair of enantiomeric ligands: S enantiomer

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-27
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0000
Spacegroup name	P 21 21 21
Unit cell lengths	36.388, 57.814, 62.586
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.460 - 1.160
R-factor	0.1274
Rwork	0.126
R-free	0.15620
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3zsj
RMSD bond length	0.010
RMSD bond angle	1.116
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX
Refinement software	PHENIX (1.14_3247)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.460	1.200
High resolution limit [Å]	1.160	1.160
Rmerge	0.059	0.756
Rmeas	0.065	0.903
Rpim	0.027	0.487
Number of reflections	46420	4567
<I/σ(I)>	19.1	1.7
Completeness [%]	99.9	99.6
Redundancy	5.5	3.3
CC(1/2)	0.999	0.618

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	295	Hanging drop vapour diffusion: 28% (w/v) PEG 4000, Tris-HCl pH 7.5, 0.4 M NaSCN, 15 mM beta-mercaptoethanol. The drop volume was 2 microlitres and the protein solution:reservoir ratio was varied between 0.5:1, 1:1, and 2:1. The crystals were soaked in 10 mM of the ligand for 20 hours.