1OEM

PTP1B with the catalytic cysteine oxidized to a sulfenyl-amide bond


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.50.1M HEPES PH 7.5, 12%PEG, 0.2M MGCL2. PROTEIN WAS OXIDIZED WITH A 1:1.25 MOLAR RATIO OF H2O2 - PROTEIN PRIOR TO CRYSTALLIZATION
Crystal Properties
Matthews coefficientSolvent content
3.7366.75

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 88.218α = 90
b = 88.218β = 90
c = 103.787γ = 120
Symmetry
Space GroupP 31 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC CCD2002-07-15MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONESRF BEAMLINE ID14-1ESRFID14-1

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
11.755099.50.03926.267.0743606
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)
11.81.8499.30.35526.26

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 2HNP1.876.741389221799.50.2040.2030.227RANDOM27.7
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]
0.690.340.69-1.03
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg6.098
r_angle_refined_deg1.836
r_nbd_refined0.211
r_symmetry_hbond_refined0.195
r_symmetry_vdw_refined0.176
r_xyhbond_nbd_refined0.149
r_chiral_restr0.14
r_bond_refined_d0.02
r_gen_planes_refined0.008
r_bond_other_d
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg6.098
r_angle_refined_deg1.836
r_nbd_refined0.211
r_symmetry_hbond_refined0.195
r_symmetry_vdw_refined0.176
r_xyhbond_nbd_refined0.149
r_chiral_restr0.14
r_bond_refined_d0.02
r_gen_planes_refined0.008
r_bond_other_d
r_angle_other_deg
r_dihedral_angle_2_deg
r_dihedral_angle_3_deg
r_dihedral_angle_4_deg
r_gen_planes_other
r_nbd_other
r_nbtor_refined
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_it
r_mcbond_other
r_mcangle_it
r_mcangle_other
r_scbond_it
r_scbond_other
r_scangle_it
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 Atoms2289
Nucleic Acid Atoms
Solvent Atoms181
Heterogen Atoms

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing