7CXC

Structure of mouse Galectin-3 CRD point mutant (V160A) in complex with TD-139 belonging to P121 space group.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP		293.15	24-35% PEG 4000/6000, 0.1M Tris (pH 7.5 to pH 8.5), 0.4M NaSCN

Crystal Properties
Matthews coefficient	Solvent content
1.84	33.16

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 35.513	α = 90
b = 58.286	β = 103.56
c = 68.085	γ = 90

Symmetry
Space Group	P 1 21 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	PIXEL	DECTRIS EIGER2 X 9M		2016-12-17	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-D	1.12713	APS	21-ID-D

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	CC (Half)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.4	58.29	77.7	0.044	0.053	0.029	0.994	16.9	3.2		53247

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.14	1.2	17.6		0.159	0.22	0.151	0.953		2

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	7CXB	1.4	43.74	48248	2566	95.43	0.1459	0.1442	0.1782	RANDOM	14.564

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
-3.85		2.2	2.78		1.07

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.302
r_dihedral_angle_3_deg	12.053
r_dihedral_angle_4_deg	11.094
r_dihedral_angle_1_deg	7.942
r_rigid_bond_restr	4.297
r_angle_refined_deg	2.023
r_angle_other_deg	0.76
r_chiral_restr	0.127
r_bond_refined_d	0.018
r_gen_planes_refined	0.014

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.302
r_dihedral_angle_3_deg	12.053
r_dihedral_angle_4_deg	11.094
r_dihedral_angle_1_deg	7.942
r_rigid_bond_restr	4.297
r_angle_refined_deg	2.023
r_angle_other_deg	0.76
r_chiral_restr	0.127
r_bond_refined_d	0.018
r_gen_planes_refined	0.014
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2126
Nucleic Acid Atoms
Solvent Atoms	258
Heterogen Atoms	300

Software

Software
Software Name	Purpose
REFMAC	refinement
Aimless	data scaling
PDB_EXTRACT	data extraction
MOSFLM	data reduction
PHASER	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.