2FHS

Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP729322% PEG 4000 and 1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
Crystal Properties
Matthews coefficientSolvent content
3.6866.6

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 127.74α = 90
b = 127.74β = 90
c = 206.73γ = 120
Symmetry
Space GroupP 65 2 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC QUANTUM 42003-06-22MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONNSLS BEAMLINE X26C0.97830NSLSX26C

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (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
12.75097.1281382731122
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
12.72.898.4

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Cut-off Sigma (F)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT2.730225906137997.320.226140.224110.26293RANDOM58.385
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]
-1.29-0.65-1.291.94
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.749
r_dihedral_angle_3_deg16.942
r_dihedral_angle_4_deg16.156
r_dihedral_angle_1_deg5.919
r_scangle_it2.053
r_scbond_it1.275
r_angle_refined_deg1.235
r_mcangle_it1.068
r_mcbond_it0.588
r_nbtor_refined0.302
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.749
r_dihedral_angle_3_deg16.942
r_dihedral_angle_4_deg16.156
r_dihedral_angle_1_deg5.919
r_scangle_it2.053
r_scbond_it1.275
r_angle_refined_deg1.235
r_mcangle_it1.068
r_mcbond_it0.588
r_nbtor_refined0.302
r_nbd_refined0.218
r_symmetry_vdw_refined0.18
r_xyhbond_nbd_refined0.178
r_symmetry_hbond_refined0.102
r_chiral_restr0.081
r_bond_refined_d0.01
r_gen_planes_refined0.004
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_other
r_nbtor_other
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_other
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 Atoms3941
Nucleic Acid Atoms
Solvent Atoms79
Heterogen Atoms

Software

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