3EJ2

Crystal structure of inorganic pyrophosphatase from burkholderia pseudomallei with bound 5-amino-1-(4-chlorophenyl)-1h-pyrazole-4-carbonitrile, H32 crystal form


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, SITTING DROP5.4289100 MM IMIDAZOLE, PH 5.4, 20% PEG 3500, 100 MM SODIUM THIOCYANATE, 12.5 MM 5-AMINO-1-(4- CHLOROPHENYL)-1H-PYRAZOLE-4-CARBONITRILE, , pH 5.40, VAPOR DIFFUSION, SITTING DROP, temperature 289K
Crystal Properties
Matthews coefficientSolvent content
2.0339.55

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 68.496α = 90
b = 68.496β = 90
c = 193.565γ = 120
Symmetry
Space GroupH 3 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCD2008-08-31MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONALS BEAMLINE 5.0.10.99987ALS5.0.1

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Merge I (Observed)Net I Over Average Sigma (I)RedundancyNumber Reflections (All)Number Reflections (Observed)Observed Criterion Sigma (F)Observed Criterion Sigma (I)B (Isotropic) From Wilson Plot
12.15097.80.0829.37.410287
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R Merge I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
12.12.1878.30.5724

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT2.1250102874970.2050.2030.249RANDOM35.66
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]
-0.31-0.15-0.310.46
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg33.94
r_dihedral_angle_4_deg30.482
r_dihedral_angle_3_deg14.698
r_dihedral_angle_1_deg6
r_scangle_it3.354
r_scbond_it1.962
r_angle_refined_deg1.784
r_mcangle_it1.341
r_mcbond_it0.727
r_chiral_restr0.092
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg33.94
r_dihedral_angle_4_deg30.482
r_dihedral_angle_3_deg14.698
r_dihedral_angle_1_deg6
r_scangle_it3.354
r_scbond_it1.962
r_angle_refined_deg1.784
r_mcangle_it1.341
r_mcbond_it0.727
r_chiral_restr0.092
r_bond_refined_d0.011
r_gen_planes_refined0.007
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_refined
r_nbd_other
r_nbtor_refined
r_nbtor_other
r_xyhbond_nbd_refined
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_refined
r_symmetry_vdw_other
r_symmetry_hbond_refined
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms1393
Nucleic Acid Atoms
Solvent Atoms66
Heterogen Atoms15

Software

Software
Software NamePurpose
HKL-2000data collection
MOLREPphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling