1O8N

The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
16.51.4 M SODIUM ACETATE 0.1 M SODIUM CACODYLATE, PH 6.5
Crystal Properties
Matthews coefficientSolvent content
2.956.5

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 122.486α = 90
b = 122.486β = 90
c = 174.36γ = 90
Symmetry
Space GroupI 41 2 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATERIGAKU IMAGE PLATEOSMIX MIRROR2001-07-18MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RU200

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
12.887.7199.70.0746.65.215774
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)
12.82.951000.1574.45.2

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 1EAV2.81001577384499.50.1960.1940.231RANDOM42.67
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]
-0.45-0.450.89
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg5.001
r_scangle_it4.171
r_scbond_it2.181
r_mcangle_it1.575
r_angle_refined_deg1.488
r_angle_other_deg0.846
r_mcbond_it0.801
r_symmetry_vdw_other0.332
r_nbd_other0.249
r_nbd_refined0.231
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg5.001
r_scangle_it4.171
r_scbond_it2.181
r_mcangle_it1.575
r_angle_refined_deg1.488
r_angle_other_deg0.846
r_mcbond_it0.801
r_symmetry_vdw_other0.332
r_nbd_other0.249
r_nbd_refined0.231
r_symmetry_hbond_refined0.206
r_xyhbond_nbd_refined0.173
r_symmetry_vdw_refined0.157
r_nbtor_other0.087
r_chiral_restr0.072
r_bond_refined_d0.014
r_gen_planes_refined0.004
r_bond_other_d0.002
r_gen_planes_other0.002
r_dihedral_angle_2_deg
r_dihedral_angle_3_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 Atoms3582
Nucleic Acid Atoms
Solvent Atoms49
Heterogen Atoms

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing