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1AUP

GLUTAMATE DEHYDROGENASE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.5
Synchrotron siteSRS
BeamlinePX9.5
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1993-10-12
DetectorMARRESEARCH
Spacegroup nameH 3 2
Unit cell lengths162.900, 162.900, 100.700
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution18.000 - 2.500
Rwork0.190
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)CLOSTRIDIUM SYMBIOSUM GLUTAMATE DEHYDROGENASE (WILD TYPE) CRYSTALLIZED WITH SODIUM GLUTAMATE IN SPACE GROUP R32. ALL WATERS AND THE BOUND GLUTAMATE SUBSTRATE REMOVED.
RMSD bond length0.017
RMSD bond angle18.600

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareTFFC
Refinement softwareTNT (5E)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]18.0002.570
High resolution limit [Å]2.5002.500
Rmerge0.070

*

0.310
Total number of observations90734

*

Number of reflections17791
<I/σ(I)>9.52.4
Completeness [%]99.099
Redundancy5.15.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

7.3

*

pH 7.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropsodium glutamate1.0 (M)
31droppotassium phosphate0.1 (M)
41reservoirpotassium phosphate0.1 (M)
51reservoirammonium sulfate38-46 (%)

223532

PDB entries from 2024-08-07

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