4H3U

Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	0.05 M Cadmium Sulfate, 0.1 M Hepes, 0.5 M Sodium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.29	46.38

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 61.578	α = 90
b = 61.578	β = 90
c = 144.576	γ = 120

Symmetry
Space Group	P 61

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	MIRROR	2012-08-13	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-G	0.97857	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	1.15	50	97.4	0.05	34.7	5.8	212580	212580		-3	14.6

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	1.15	1.17	95.7		0.5	2.8	5.6	10416

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	SAD	THROUGHOUT	1.15	29.94	104170	104170	5480	99.94	0.12909	0.12835	0.14313	RANDOM	14.577

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]
0.86	0.86		0.86		-2.79

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	56.165
r_dihedral_angle_2_deg	33.364
r_dihedral_angle_4_deg	18.542
r_sphericity_bonded	14.243
r_dihedral_angle_3_deg	9.225
r_dihedral_angle_1_deg	4.531
r_rigid_bond_restr	4.23
r_angle_refined_deg	1.719
r_angle_other_deg	0.821
r_chiral_restr	0.095

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	56.165
r_dihedral_angle_2_deg	33.364
r_dihedral_angle_4_deg	18.542
r_sphericity_bonded	14.243
r_dihedral_angle_3_deg	9.225
r_dihedral_angle_1_deg	4.531
r_rigid_bond_restr	4.23
r_angle_refined_deg	1.719
r_angle_other_deg	0.821
r_chiral_restr	0.095
r_bond_refined_d	0.014
r_gen_planes_refined	0.011
r_gen_planes_other	0.003
r_bond_other_d	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1955
Nucleic Acid Atoms
Solvent Atoms	417
Heterogen Atoms	30

Software

Software
Software Name	Purpose
Blu-Ice	data collection
HKL-3000	phasing
REFMAC	refinement
HKL-3000	data reduction
HKL-3000	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 R01GM157729.