1PKZ

Crystal structure of human glutathione transferase (GST) A1-1


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP8.5293MethylPEG2000, Tris-HCl, NaAc, 2-mercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystal Properties
Matthews coefficientSolvent content
2.2144.28

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 99α = 90
b = 89.888β = 93.28
c = 51.082γ = 90
Symmetry
Space GroupC 1 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATEMARRESEARCH2000-05-10MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONMAX II BEAMLINE I7110.9831MAX III711

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
12.1252611125470-3
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
2.12.1896.9

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (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 REPLACEMENTTHROUGHOUT2.165.942547022897257397.550.18560.180550.2298RANDOM25.164
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]
-0.480.561.18-0.64
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg6.01
r_scangle_it3.273
r_scbond_it2.038
r_angle_refined_deg1.461
r_mcangle_it1.435
r_angle_other_deg1.04
r_mcbond_it0.798
r_nbd_other0.236
r_nbd_refined0.216
r_symmetry_vdw_refined0.184
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg6.01
r_scangle_it3.273
r_scbond_it2.038
r_angle_refined_deg1.461
r_mcangle_it1.435
r_angle_other_deg1.04
r_mcbond_it0.798
r_nbd_other0.236
r_nbd_refined0.216
r_symmetry_vdw_refined0.184
r_xyhbond_nbd_refined0.175
r_symmetry_vdw_other0.153
r_symmetry_hbond_refined0.133
r_nbtor_other0.097
r_chiral_restr0.085
r_bond_refined_d0.016
r_gen_planes_refined0.006
r_gen_planes_other0.004
r_bond_other_d0.002
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_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms3500
Nucleic Acid Atoms
Solvent Atoms300
Heterogen Atoms16

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing