2A9B

Crystal structure of R138Q mutant of recombinant sulfite oxidase at resting state

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.5	295	PEG 4000, magnesium chloride, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
3.52	64.76

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 86.109	α = 90
b = 86.109	β = 90
c = 153.825	γ = 90

Symmetry
Space Group	I 41

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	ADSC QUANTUM 4		2003-08-20	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X26C	1.100	NSLS	X26C

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	2.5	30	100	0.089				19275

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	2.5	2.59	100	100	0.599

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-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	FOURIER SYNTHESIS	THROUGHOUT	PDB ENTRY 2A99	2.503	30	19258	947	99.84	0.158	0.158	0.156	0.202	Copied from R-free of reflections of wild type crystals (PDB Entry 2A99)	42.854

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]
1.7			1.7		-3.4

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.28
r_dihedral_angle_4_deg	18.154
r_dihedral_angle_3_deg	13.87
r_dihedral_angle_1_deg	3.717
r_scangle_it	2.93
r_scbond_it	1.692
r_angle_refined_deg	1.488
r_mcangle_it	1.31
r_mcbond_it	0.724
r_nbtor_refined	0.328

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	29.28
r_dihedral_angle_4_deg	18.154
r_dihedral_angle_3_deg	13.87
r_dihedral_angle_1_deg	3.717
r_scangle_it	2.93
r_scbond_it	1.692
r_angle_refined_deg	1.488
r_mcangle_it	1.31
r_mcbond_it	0.724
r_nbtor_refined	0.328
r_nbd_refined	0.22
r_xyhbond_nbd_refined	0.218
r_symmetry_hbond_refined	0.204
r_metal_ion_refined	0.198
r_symmetry_vdw_refined	0.141
r_chiral_restr	0.09
r_bond_refined_d	0.01
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2869
Nucleic Acid Atoms
Solvent Atoms	215
Heterogen Atoms	26

Software

Software
Software Name	Purpose
HKL-2000	data collection
HKL-2000	data reduction
REFMAC	refinement
HKL-2000	data scaling

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.