3CMT

Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
18the RecA5 fusion protein was incubated with a 1.5-fold molar excess of the primary d(T5C3AC2T4) oligonucleotide in protein buffer supplemented with 2 mM ADP, 10 mM MgCl2 and 8 mM AlF4, pH 6.0, for 30 min, followed by the addition of 2-fold molar excess of the complementary d(G2TG3) oligonucleotide. The crystals grew from 50 mM Tris-Cl, 9% (w/v) PVP K15, 32% (v/v) MPD, 100 mM magnesium acetate, 10 mM DTT, pH 8.0.
Crystal Properties
Matthews coefficientSolvent content
2.5451.51

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 159α = 90
b = 300.5β = 90
c = 80.1γ = 90
Symmetry
Space GroupP 21 21 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray2007-07-01MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONAPS BEAMLINE 24-ID-CAPS24-ID-C

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
13.154059390

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 REPLACEMENTTHROUGHOUT3.154059390123189.90.2180.2170.243RANDOM50.72
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]
1.53-0.63-0.91
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.392
r_dihedral_angle_3_deg19.073
r_dihedral_angle_4_deg15.721
r_dihedral_angle_1_deg5.156
r_scangle_it2.706
r_scbond_it1.643
r_mcangle_it1.498
r_angle_refined_deg1.17
r_mcbond_it0.845
r_symmetry_hbond_refined0.559
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg36.392
r_dihedral_angle_3_deg19.073
r_dihedral_angle_4_deg15.721
r_dihedral_angle_1_deg5.156
r_scangle_it2.706
r_scbond_it1.643
r_mcangle_it1.498
r_angle_refined_deg1.17
r_mcbond_it0.845
r_symmetry_hbond_refined0.559
r_symmetry_vdw_refined0.421
r_nbtor_refined0.307
r_nbd_refined0.201
r_xyhbond_nbd_refined0.125
r_chiral_restr0.073
r_metal_ion_refined0.056
r_bond_refined_d0.008
r_gen_planes_refined0.003
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_other
r_nbtor_other
r_xyhbond_nbd_other
r_metal_ion_other
r_symmetry_vdw_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms24250
Nucleic Acid Atoms732
Solvent Atoms
Heterogen Atoms330

Software

Software
Software NamePurpose
REFMACrefinement