2BWV

His361Ala Escherichia coli Aminopeptidase P


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP8.5277HANGING DROP VAPOUR DIFFUSION AT 4C. 2 UL 6 MG/ML APPRO PLUS 2 UL RESERVOIR SOLUTION: 28 % PEG 4K, 0.1 M TRIS PH 8.5. SOAKED IN RESERVOIR SOLUTION SUPPLEMENTED WITH 10% MPD AND 1 MM MNCL2 FOR 1 HR AT 4C PRIOR TO CRYOCOOLING.
Crystal Properties
Matthews coefficientSolvent content
4.471.9

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 177.339α = 90
b = 177.339β = 90
c = 96.475γ = 120
Symmetry
Space GroupP 64 2 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATEMARRESEARCHOSMIC MIRRORS2005-04-05MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RU200H

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
11.765.2399.40.0619.7696986622.44
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)
11.71.7999.50.482.85.1

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 1WL91.7154.394042293899.20.150.150.165RANDOM21.04
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]
-0.08-0.04-0.080.12
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.828
r_dihedral_angle_4_deg15.314
r_dihedral_angle_3_deg10.772
r_dihedral_angle_1_deg5.902
r_scangle_it5.594
r_scbond_it3.857
r_mcangle_it2.265
r_mcbond_it2.027
r_angle_refined_deg1.206
r_angle_other_deg0.803
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.828
r_dihedral_angle_4_deg15.314
r_dihedral_angle_3_deg10.772
r_dihedral_angle_1_deg5.902
r_scangle_it5.594
r_scbond_it3.857
r_mcangle_it2.265
r_mcbond_it2.027
r_angle_refined_deg1.206
r_angle_other_deg0.803
r_symmetry_vdw_other0.307
r_symmetry_vdw_refined0.228
r_nbd_refined0.21
r_nbd_other0.176
r_nbtor_refined0.172
r_xyhbond_nbd_refined0.114
r_symmetry_hbond_refined0.11
r_nbtor_other0.079
r_chiral_restr0.074
r_bond_refined_d0.01
r_gen_planes_refined0.005
r_bond_other_d0.001
r_gen_planes_other0.001
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_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 Atoms3495
Nucleic Acid Atoms
Solvent Atoms649
Heterogen Atoms3

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALEPACKdata scaling