2WF7

Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphonate and Aluminium tetrafluoride


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.219-21 % PEG 3350 AND 50 MM MG ACETATE, pH 7.2
Crystal Properties
Matthews coefficientSolvent content
1.8633.51

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 37.5α = 90
b = 54.3β = 90
c = 104.7γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC CCDGE211MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONESRF BEAMLINE ID14-2ESRFID14-2

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
11.052089.20.067.62.3892133
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)
11.051.08550.221.61.3

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 REPLACEMENTTHROUGHOUT1.052084669444888.80.1540.1530.176RANDOM
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]
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.135
r_dihedral_angle_4_deg21.681
r_dihedral_angle_3_deg12.187
r_dihedral_angle_1_deg5.511
r_sphericity_free4.433
r_sphericity_bonded3.594
r_scangle_it3.184
r_scbond_it2.047
r_mcangle_it1.5
r_angle_refined_deg1.383
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.135
r_dihedral_angle_4_deg21.681
r_dihedral_angle_3_deg12.187
r_dihedral_angle_1_deg5.511
r_sphericity_free4.433
r_sphericity_bonded3.594
r_scangle_it3.184
r_scbond_it2.047
r_mcangle_it1.5
r_angle_refined_deg1.383
r_angle_other_deg1.169
r_mcbond_it0.942
r_rigid_bond_restr0.913
r_mcbond_other0.542
r_chiral_restr0.206
r_bond_refined_d0.009
r_gen_planes_refined0.007
r_bond_other_d0.002
r_gen_planes_other0.001
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_other
r_long_range_B_refined
r_long_range_B_other
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms1680
Nucleic Acid Atoms
Solvent Atoms285
Heterogen Atoms23

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing