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1H93

ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1995-11-12
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths129.330, 44.280, 91.170
Unit cell angles90.00, 105.39, 90.00
Refinement procedure
Resolution25.000 - 2.200
R-factor0.206
Rwork0.206
R-free0.28200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)SUBUNIT 'A' OF 1DPG
RMSD bond length0.005
RMSD bond angle22.460

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.280
High resolution limit [Å]2.2002.200
Rmerge0.081

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0.298

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Total number of observations57502

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Number of reflections247102148

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<I/σ(I)>12.62.9
Completeness [%]96.485.2
Redundancy2.32
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5291

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HANGING DROP VAPOUR DIFFUSION, 2+2 MICROLITER DROPS. THE WELL BUFFER: 20% V/V PEG 400 IN 0.1M HEPES-NAOH, PH 7.5 WITH 0.2M CALCIUM CHLORIDE. THE PROTEIN AT 10MG/ML IN 100MM TRIS-HCL WITH 12.5MM NAD+.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG40020 (%(v/v))
21reservoirHEPES-NaOH0.1 (M)
31reservoir200 (mM)
41dropprotein10 (mg/ml)
51dropTris-HCl100 (mM)
61dropNAD+12.5 (mM)

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