2IIK

Crystal Structure of human peroxisomal acetyl-CoA acyl transferase 1 (ACAA1)


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, SITTING DROP7.52980.2M Amonium Sulphate, 0.1M Hepes, 25% PEG3350., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Crystal Properties
Matthews coefficientSolvent content
2.1642.94

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 55.147α = 90
b = 96.845β = 90
c = 142.055γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATERIGAKU RAXIS HTC2006-07-27MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU

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
12.5580.06990.10999.653.662562425358
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)
12.552.6596.20.4012.172.792760

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (High)Resolution (Low)Number Reflections (All)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT2C7Z2.5580.0625624240371274990.181080.178690.22345RANDOM21.615
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]
-0.821.76-0.94
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.375
r_dihedral_angle_4_deg15.936
r_dihedral_angle_3_deg15.782
r_dihedral_angle_1_deg6.42
r_scangle_it2.314
r_scbond_it1.516
r_angle_refined_deg1.402
r_angle_other_deg1.192
r_mcangle_it0.733
r_mcbond_it0.487
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.375
r_dihedral_angle_4_deg15.936
r_dihedral_angle_3_deg15.782
r_dihedral_angle_1_deg6.42
r_scangle_it2.314
r_scbond_it1.516
r_angle_refined_deg1.402
r_angle_other_deg1.192
r_mcangle_it0.733
r_mcbond_it0.487
r_symmetry_vdw_refined0.223
r_nbd_refined0.217
r_nbd_other0.195
r_symmetry_vdw_other0.194
r_symmetry_hbond_refined0.178
r_nbtor_refined0.173
r_xyhbond_nbd_refined0.141
r_mcbond_other0.14
r_chiral_restr0.091
r_nbtor_other0.089
r_bond_refined_d0.013
r_gen_planes_refined0.004
r_bond_other_d0.002
r_gen_planes_other0.002
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_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms5639
Nucleic Acid Atoms
Solvent Atoms226
Heterogen Atoms

Software

Software
Software NamePurpose
REFMACrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MLPHAREphasing