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1E6B

Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX7.2
Synchrotron siteSRS
BeamlinePX7.2
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-10-17
DetectorMAR scanner 345 mm plate
Spacegroup nameP 65 2 2
Unit cell lengths75.164, 75.164, 140.520
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.000 - 1.650
R-factor0.196

*

Rwork0.196
R-free0.23400
Structure solution methodSIRAS
RMSD bond length0.011
RMSD bond angle1.600

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCCP4
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0001.690
High resolution limit [Å]1.6501.650
Rmerge0.040
Number of reflections150341
Completeness [%]94.795.9
Redundancy5-6

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.515

*

11% PEG 8000, 0.2M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLA, pH 7.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21dropTris-HCl20 (mM)
31reservoirPEG800011 (%(w/v))
41reservoirmagnesium acetate0.2 (M)
51reservoirsodium cacodylate0.1 (M)

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PDB entries from 2024-05-15

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