4F3N

High resolution native crystal structure of an uncharacterized ACR, COG1565 superfamily protein from Burkholderia thailandensis, solved by iodide ion SAD

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	ButhA.17973.a.A1 PS01383 at 21.5 mg/mL against JCSG+ H7 0.2 M ammonium sulfate, 0.1 M BisTris pH 5.5, 25% PEG 3350 with 20% ethylene glycol as cryo-protectant, crystal tracking ID 231359h7, PEGasIS iodide soak 1M NaI/20EG, VAPOR DIFFUSION, SITTING DROP, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
1.94	36.51

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 49.86	α = 90
b = 50.13	β = 90
c = 142.94	γ = 90

Symmetry
Space Group	P 21 21 21

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	RIGAKU SATURN 944+		2012-03-22	M	SINGLE WAVELENGTH
2	1	100	CCD	ADSC QUANTUM 315r		2012-04-27
3	1	x-ray		M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU FR-E+ SUPERBRIGHT	1.5418
2	SYNCHROTRON	SSRL BEAMLINE BL7-1	1.377552	SSRL	BL7-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	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
1,3	1.75	50	99.5	0.042	26.89	5.1	37042	36871		-3	22.921

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1,3	1.75	1.8	96		0.34	3.28

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	SAD	THROUGHOUT	1.75	50	36871	1842	99.54	0.1687	0.1671	0.1988	RANDOM	18.1606

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]
-0.46			-0.02		0.48

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.725
r_dihedral_angle_4_deg	14.88
r_dihedral_angle_3_deg	11.745
r_dihedral_angle_1_deg	5.968
r_angle_refined_deg	1.474
r_angle_other_deg	0.938
r_chiral_restr	0.092
r_bond_refined_d	0.013
r_gen_planes_refined	0.007
r_gen_planes_other	0.002

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.725
r_dihedral_angle_4_deg	14.88
r_dihedral_angle_3_deg	11.745
r_dihedral_angle_1_deg	5.968
r_angle_refined_deg	1.474
r_angle_other_deg	0.938
r_chiral_restr	0.092
r_bond_refined_d	0.013
r_gen_planes_refined	0.007
r_gen_planes_other	0.002
r_bond_other_d	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2746
Nucleic Acid Atoms
Solvent Atoms	270
Heterogen Atoms	14

Software

Software
Software Name	Purpose
XSCALE	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
XDS	data reduction

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.