1H4X

Structure of the Bacillus Cell Fate Determinant SpoIIAA in the Phosphorylated Form


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
16.530% PEG 5K MME, 200MM (NH4)2SO4, 100MM MES (PH 6.5)
Crystal Properties
Matthews coefficientSolvent content
1.9637.35

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 51.119α = 90
b = 61.577β = 90
c = 65.892γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC CCDMSINGLE 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
11.162097.90.06818.93.872227
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)
11.161.285.40.33.722.5

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT1.1619.6168102362698.80.1330.164RANDOM
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]
RMS Deviations
KeyRefinement Restraint Deviation
r_scangle_it4.738
r_scbond_it3.395
r_mcangle_it2.666
r_angle_other_deg2.086
r_mcbond_it1.834
r_nbtor_other1.047
r_dihedral_angle_3_deg0.922
r_nbd_refined0.268
r_xyhbond_nbd_refined0.259
r_nbd_other0.245
RMS Deviations
KeyRefinement Restraint Deviation
r_scangle_it4.738
r_scbond_it3.395
r_mcangle_it2.666
r_angle_other_deg2.086
r_mcbond_it1.834
r_nbtor_other1.047
r_dihedral_angle_3_deg0.922
r_nbd_refined0.268
r_xyhbond_nbd_refined0.259
r_nbd_other0.245
r_symmetry_vdw_other0.234
r_symmetry_hbond_refined0.224
r_symmetry_vdw_refined0.213
r_chiral_restr0.129
r_bond_refined_d0.024
r_gen_planes_refined0.009
r_gen_planes_other0.003
r_bond_other_d0.001
r_angle_refined_deg
r_dihedral_angle_1_deg
r_dihedral_angle_2_deg
r_dihedral_angle_4_deg
r_nbtor_refined
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 Atoms1768
Nucleic Acid Atoms
Solvent Atoms426
Heterogen Atoms16

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing