4Q4T

Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at E444


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP4.62938 mg mL-1 protein concentration and 2.0 M sodium formate in 0.1 M sodium acetate trihydrate buffer, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 36.711α = 90
b = 65.27β = 90
c = 68.195γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDRIGAKU SATURN 9442013-04-15MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU1.54

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (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
11.633098.52118020862
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
11.631.6677.3

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 REPLACEMENTTHROUGHOUT1.631519279104796.320.137960.135490.18678RANDOM14.521
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]
0.10.27-0.37
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg32.904
r_dihedral_angle_3_deg12.274
r_dihedral_angle_4_deg10.249
r_dihedral_angle_1_deg6.332
r_scangle_it5.003
r_scbond_it3.151
r_mcangle_it2.044
r_angle_refined_deg2.04
r_mcbond_it1.289
r_chiral_restr0.287
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg32.904
r_dihedral_angle_3_deg12.274
r_dihedral_angle_4_deg10.249
r_dihedral_angle_1_deg6.332
r_scangle_it5.003
r_scbond_it3.151
r_mcangle_it2.044
r_angle_refined_deg2.04
r_mcbond_it1.289
r_chiral_restr0.287
r_bond_refined_d0.027
r_gen_planes_refined0.012
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
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_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 Atoms1539
Nucleic Acid Atoms
Solvent Atoms259
Heterogen Atoms18

Software

Software
Software NamePurpose
REFMACrefinement