2XC1

Full-length Tailspike Protein Mutant Y108W of Bacteriophage P22


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP7292PROTEIN- 15MG/ML IN 10MM HEPES PH7;RESERVOIR:750 ML 0.2M AMMONIUM ACETATE,0.1M TRI-SODIUM CITRATE DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE GLYCOL 4000; HANGING DROPS:1.5MICROL RESERVOIR- 1.5MICROL PROTEIN SOLUTION; TEMPERATURE: 19 DEGR.; CRYO: 3% GLYCEROL
Crystal Properties
Matthews coefficientSolvent content
2.5151.1

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 86.358α = 90
b = 121.558β = 90
c = 208.255γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDMARMOSAIC 225 mm CCDMIRRORS2008-02-28MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONBESSY BEAMLINE 14.1BESSY14.1

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
11.6548.390.40.112.56.3237282-320
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)
11.651.8568.30.452.32.8

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 ENTRIES 2VNL AND 2VFM1.6549.452287711204191.730.167560.165320.21038RANDOM8.822
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]
-0.010.05-0.04
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.059
r_dihedral_angle_4_deg12.401
r_dihedral_angle_3_deg12.303
r_dihedral_angle_1_deg6.619
r_scangle_it5.315
r_scbond_it3.834
r_mcangle_it2.508
r_mcbond_it1.791
r_angle_refined_deg1.366
r_angle_other_deg0.836
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.059
r_dihedral_angle_4_deg12.401
r_dihedral_angle_3_deg12.303
r_dihedral_angle_1_deg6.619
r_scangle_it5.315
r_scbond_it3.834
r_mcangle_it2.508
r_mcbond_it1.791
r_angle_refined_deg1.366
r_angle_other_deg0.836
r_mcbond_other0.658
r_chiral_restr0.084
r_bond_refined_d0.012
r_gen_planes_refined0.006
r_bond_other_d0.001
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
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms15064
Nucleic Acid Atoms
Solvent Atoms2265
Heterogen Atoms131

Software

Software
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
AMoREphasing