7ZSI

Structure of Orange Carotenoid Protein with canthaxanthin bound after 5 minutes of illumination

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	4XB5

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	100 mM sodium acetate pH 4.5, 10 % poly-ethylene glycol 20,000, 3 % glycerol

Crystal Properties
Matthews coefficient	Solvent content
2.53	51.41

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 82.78	α = 90
b = 82.78	β = 90
c = 87.604	γ = 120

Symmetry
Space Group	P 32 2 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 XE 16M		2019-07-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	DIAMOND BEAMLINE I03	0.9795	Diamond	I03

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	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	1.399	55.542	100	0.133	0.14	0.044	14.4	19.8		68765

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.4	1.44			9.9	11.51	3.645

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 (All)	R-Work	R-Free	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	4XB5	1.399	55.542	68710	3410	99.897	0.192	0.1912	0.2048	25.71

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]
0.009	0.004		0.009		-0.029

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.548
r_dihedral_angle_4_deg	20.007
r_dihedral_angle_3_deg	13.19
r_lrange_it	7.245
r_dihedral_angle_1_deg	5.821
r_scangle_it	4.051
r_mcangle_it	3.099
r_scbond_it	2.774
r_mcbond_it	2.072
r_angle_refined_deg	1.738

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.548
r_dihedral_angle_4_deg	20.007
r_dihedral_angle_3_deg	13.19
r_lrange_it	7.245
r_dihedral_angle_1_deg	5.821
r_scangle_it	4.051
r_mcangle_it	3.099
r_scbond_it	2.774
r_mcbond_it	2.072
r_angle_refined_deg	1.738
r_symmetry_xyhbond_nbd_refined	0.365
r_nbtor_refined	0.311
r_xyhbond_nbd_refined	0.269
r_symmetry_nbd_refined	0.229
r_nbd_refined	0.212
r_chiral_restr	0.104
r_bond_refined_d	0.011
r_gen_planes_refined	0.011

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2411
Nucleic Acid Atoms
Solvent Atoms	400
Heterogen Atoms	53

Software

Software
Software Name	Purpose
REFMAC	refinement
DIALS	data reduction
DIALS	data scaling
MOLREP	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 R01GM157729.