2BXR

Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
16.5PROTEIN WAS CRYSTALLIZED FROM 6% PEG 6000, 100 MM LISULPHATE, 100 MM NACITRATE, 50 MM KPI PH 7.0.
Crystal Properties
Matthews coefficientSolvent content
2.6645

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 143.493α = 90
b = 109.599β = 95.18
c = 81.329γ = 90
Symmetry
Space GroupC 1 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray1002005-02-14MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONAPS BEAMLINE 22-IDAPS22-ID

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
131596.90.016.723085
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)
133.197.30.526.2

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 1S2Q387.0423085124596.50.1950.1920.238RANDOM63.9
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]
5.821.86-3.67-1.82
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg37.414
r_dihedral_angle_4_deg22.894
r_dihedral_angle_3_deg21.175
r_dihedral_angle_1_deg6.385
r_angle_refined_deg1.696
r_scangle_it1.609
r_scbond_it1.084
r_mcangle_it0.585
r_symmetry_vdw_refined0.366
r_mcbond_it0.338
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg37.414
r_dihedral_angle_4_deg22.894
r_dihedral_angle_3_deg21.175
r_dihedral_angle_1_deg6.385
r_angle_refined_deg1.696
r_scangle_it1.609
r_scbond_it1.084
r_mcangle_it0.585
r_symmetry_vdw_refined0.366
r_mcbond_it0.338
r_nbtor_refined0.326
r_nbd_refined0.251
r_xyhbond_nbd_refined0.176
r_chiral_restr0.103
r_symmetry_hbond_refined0.1
r_bond_refined_d0.018
r_gen_planes_refined0.005
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_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_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 Atoms7046
Nucleic Acid Atoms
Solvent Atoms
Heterogen Atoms140

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing