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1H9B

ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1994-11-15
DetectorMARRESEARCH
Spacegroup nameP 62 2 2
Unit cell lengths136.700, 136.700, 121.200
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution21.000 - 2.400
R-factor0.19
Rwork0.190
R-free0.23600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)PROTEIN ATOMS OF NADP-BOUND COMPLEX IN THE SAME CRYSTAL FORM 1H9A.
RMSD bond length0.006
RMSD bond angle22.730

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Data reduction softwareDENZO
Data scaling softwareSCALA
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]21.0002.530
High resolution limit [Å]2.4002.400
Rmerge0.113

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0.418

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Total number of observations115220

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Number of reflections248653523

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<I/σ(I)>12.73.7
Completeness [%]94.193
Redundancy4.65.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5

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291

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HANGING DROP VAPOUR DIFFUSION, 2+2 MICROLITER DROPS. THE PROTEIN AT 5MG/ML IN 100MM TRIS-HCL AT PH 7.5 WITH 12.5MM NAD+. DROPS EQUILIBRIATED AGAINST 1.7M UNBUFFERED AMMONIUM SULFATE.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
21dropTris-HCl100 (mM)
31dropNAD+12.5 (mM)
41reservoirammonium sulfate1.64 (M)unbuffered

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PDB entries from 2024-05-15

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