6TEE

Crystal structure of monooxygenase RutA under anaerobic conditions.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP		295	100 mM Bis-Tris pH 6.5, 1900 mM Ammonium Sulphate, 2-5% MPD (v/v), 1 mM FMN

Crystal Properties
Matthews coefficient	Solvent content
2.71	54.63

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 88.033	α = 90
b = 88.033	β = 90
c = 96.901	γ = 120

Symmetry
Space Group	P 31 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 EIGER X 16M		2018-06-27	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X06SA	1.0	SLS	X06SA

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	2.2	48.45	94.3	0.15	7.5	8.9		21254

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.2	2.32			0.85

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	5WAN	2.2	44.055	21126	1089	93.856	0.191	0.1888	0.2372	36.232

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]
-0.854	-0.427		-0.854		2.771

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.095
r_dihedral_angle_4_deg	17.945
r_dihedral_angle_3_deg	14.585
r_dihedral_angle_1_deg	7.122
r_lrange_it	7.079
r_scangle_it	5.843
r_scbond_it	4.144
r_mcangle_it	3.501
r_mcbond_it	2.619
r_angle_refined_deg	1.577

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.095
r_dihedral_angle_4_deg	17.945
r_dihedral_angle_3_deg	14.585
r_dihedral_angle_1_deg	7.122
r_lrange_it	7.079
r_scangle_it	5.843
r_scbond_it	4.144
r_mcangle_it	3.501
r_mcbond_it	2.619
r_angle_refined_deg	1.577
r_nbtor_refined	0.316
r_nbd_refined	0.218
r_symmetry_nbd_refined	0.209
r_symmetry_xyhbond_nbd_refined	0.137
r_chiral_restr	0.112
r_xyhbond_nbd_refined	0.109
r_bond_refined_d	0.008
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2585
Nucleic Acid Atoms
Solvent Atoms	87
Heterogen Atoms	37

Software

Software
Software Name	Purpose
REFMAC	refinement
XDS	data reduction
SCALA	data scaling
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.