2AEP

An epidemiologically significant epitope of a 1998 influenza virus neuraminidase forms a highly hydrated interface in the NA-antibody complex.


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.52M AMMONIUM SULFATE, 100 mM TRIS, pH 7.5
Crystal Properties
Matthews coefficientSolvent content
3.261.4

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 155.057α = 90
b = 155.057β = 90
c = 102.645γ = 90
Symmetry
Space GroupP 4 21 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATERIGAKU RAXIS IVOsmic2003-06-11MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Sym 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
12.12099.980.10417.646.2573146
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R-Sym I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
12.12.171000.3212.065.5

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (High)Resolution (Low)Cut-off Sigma (F)Number Reflections (All)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT1NN2, 1NCA2.1201731786945036861000.190.1880.224RANDOM32.91
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]
-0.9-0.91.79
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg7.588
r_scangle_it4.642
r_scbond_it2.996
r_angle_refined_deg1.986
r_mcangle_it1.933
r_mcbond_it1.111
r_angle_other_deg0.972
r_symmetry_vdw_other0.294
r_nbd_other0.263
r_nbd_refined0.201
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg7.588
r_scangle_it4.642
r_scbond_it2.996
r_angle_refined_deg1.986
r_mcangle_it1.933
r_mcbond_it1.111
r_angle_other_deg0.972
r_symmetry_vdw_other0.294
r_nbd_other0.263
r_nbd_refined0.201
r_symmetry_hbond_refined0.168
r_xyhbond_nbd_refined0.167
r_symmetry_vdw_refined0.134
r_chiral_restr0.127
r_metal_ion_refined0.122
r_nbtor_other0.093
r_bond_refined_d0.025
r_gen_planes_refined0.011
r_gen_planes_other0.007
r_bond_other_d0.003
r_dihedral_angle_2_deg
r_dihedral_angle_3_deg
r_dihedral_angle_4_deg
r_nbtor_refined
r_xyhbond_nbd_other
r_metal_ion_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 Atoms5125
Nucleic Acid Atoms
Solvent Atoms506
Heterogen Atoms180

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing