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1LJR

GLUTATHIONE TRANSFERASE (HGST T2-2) FROM HUMAN

Experimental procedure
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-10
DetectorMARRESEARCH
Spacegroup nameP 31 2 1
Unit cell lengths94.350, 94.350, 120.170
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution15.000 - 3.200
R-factor0.208
Rwork0.208
R-free0.30600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)L. CUPRINA GST
RMSD bond length0.008
RMSD bond angle24.900

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.8)
Refinement softwareX-PLOR (3.8)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0003.300
High resolution limit [Å]3.2003.200
Rmerge0.148

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Total number of observations27540

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Number of reflections10111
<I/σ(I)>7.43.1
Completeness [%]96.097.8
Redundancy2.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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7

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277 or 295

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drop solution was mixed with an equal volume of reservoir solution

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein1.76 (mg/ml)
21dropsodium phosphate10 (mM)
31dropbeta-mercaptoethanol1 (mM)
41reservoirPEG400015 (%)
51reservoirethanol2 (%)
61reservoirHEPES100 (mM)

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PDB entries from 2024-05-15

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