4BNU

Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (FabG) from Pseudomonas aeruginosa in complex with 2-phenyl-4-(1,2,4- triazol-4-yl)quinazoline at 2.0A resolution


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
16.50.1 M SODIUM CACODYLATE PH 6.5, 1 M TRI-SODIUM CITRATE, 1 MM 2-PHENYL-4-(1,2, 4-TRIAZOL-4-YL)QUINAZOLINE, FINAL PROTEIN CONCENTRATION 6.7 MG/ML
Crystal Properties
Matthews coefficientSolvent content
1.9938.15

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 55.3α = 90
b = 108.56β = 90
c = 148.8γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100PIXELDECTRIS PILATUS 6MMIRRORS2012-07-25MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONESRF BEAMLINE ID29ESRFID29

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
1237.4998.70.116.2460483-319.9
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)
122.0595.80.5123.2

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (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 REPLACEMENTTHROUGHOUTPDB ENTRY 4BNT CHAIN A237.5257222305898.140.203530.201220.24717RANDOM35.906
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]
2.88-2.18-0.7
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.215
r_dihedral_angle_4_deg17.701
r_dihedral_angle_3_deg14.077
r_dihedral_angle_1_deg5.653
r_mcangle_it4.303
r_scbond_it3.65
r_mcbond_it2.826
r_mcbond_other2.826
r_angle_refined_deg1.601
r_angle_other_deg1.431
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.215
r_dihedral_angle_4_deg17.701
r_dihedral_angle_3_deg14.077
r_dihedral_angle_1_deg5.653
r_mcangle_it4.303
r_scbond_it3.65
r_mcbond_it2.826
r_mcbond_other2.826
r_angle_refined_deg1.601
r_angle_other_deg1.431
r_chiral_restr0.085
r_bond_refined_d0.015
r_bond_other_d0.009
r_gen_planes_refined0.009
r_gen_planes_other0.006
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_mcangle_other
r_scbond_other
r_scangle_it
r_scangle_other
r_long_range_B_refined
r_long_range_B_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms7100
Nucleic Acid Atoms
Solvent Atoms200
Heterogen Atoms42

Software

Software
Software NamePurpose
REFMACrefinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing