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1K89

K89L MUTANT OF GLUTAMATE DEHYDROGENASE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.5
Synchrotron siteSRS
BeamlinePX9.5
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-11-23
DetectorMARRESEARCH
Spacegroup nameH 3 2
Unit cell lengths161.800, 161.800, 102.500
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution10.000 - 2.050
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)CLOSTRIDIUM SYMBIOSUM GLUTAMATE DEHYDROGENASE (WILD TYPE) CRYSTALLISED WITH SODIUM GLUTAMATE IN SPACE GROUP R32. ALL WATERS AND THE BOUND GLUTAMATE SUBSTRATE REMOVED.
RMSD bond length0.070

*

RMSD bond angle2.200

*

Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareTFFC
Refinement softwareTNT (5E)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]24.0002.100
High resolution limit [Å]2.0502.050
Rmerge0.0290.112
Total number of observations97593

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Number of reflections27219
<I/σ(I)>17.66.4
Completeness [%]84.772.7
Redundancy3.62.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7pH 7.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21dropsodium glutamate0.25 (M)
31dropsodium phosphate0.1 (M)
41dropbeta-mercaptoethanol1 (mM)
51dropEDTA1 (mM)
61reservoirammonium sulfate39.5-40.5 (%sat)

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