3OMN

Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with D132A mutation in the reduced state

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.3	277	26-29% PEG-400, pH 6.3, VAPOR DIFFUSION, SITTING DROP, reduced by dithionite, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
4.12	70.12

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 124.67	α = 90
b = 132.033	β = 90
c = 176.286	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	MARMOSAIC 300 mm CCD		2009-02-02		SINGLE WEAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-G	0.97856	APS	21-ID-G

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	2.15	50	97.5	0.086	11	7		153760

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	2.15	2.23	84		0.575		5.1	13130

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	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	2.15	42.7	153587	153587	4627	97.19	0.1985	0.1978	0.2189	RANDOM	43.9531

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]
-1.84			-0.31		2.16

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.04
r_dihedral_angle_4_deg	18.054
r_dihedral_angle_3_deg	13.643
r_dihedral_angle_1_deg	5.594
r_scangle_it	1.756
r_scbond_it	1.237
r_angle_refined_deg	1.164
r_mcangle_it	0.953
r_mcbond_it	0.574
r_nbtor_refined	0.311

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.04
r_dihedral_angle_4_deg	18.054
r_dihedral_angle_3_deg	13.643
r_dihedral_angle_1_deg	5.594
r_scangle_it	1.756
r_scbond_it	1.237
r_angle_refined_deg	1.164
r_mcangle_it	0.953
r_mcbond_it	0.574
r_nbtor_refined	0.311
r_nbd_refined	0.209
r_symmetry_vdw_refined	0.172
r_xyhbond_nbd_refined	0.123
r_metal_ion_refined	0.102
r_chiral_restr	0.086
r_symmetry_hbond_refined	0.025
r_bond_refined_d	0.011
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	12339
Nucleic Acid Atoms
Solvent Atoms	460
Heterogen Atoms	645

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
MD2	data collection
HKL-2000	data reduction
HKL-2000	data scaling
CNS	phasing

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.