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1CER

DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION

Experimental procedure
Detector technologyIMAGE PLATE
Collection date1993-05-15
DetectorRIGAKU RAXIS II
Spacegroup nameP 21 21 21
Unit cell lengths144.770, 148.770, 149.500
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution12.000 - 2.500
R-factor0.205
Rwork0.205
RMSD bond length0.021
RMSD bond angle26.320

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Data reduction softwareR-AXIS
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
High resolution limit [Å]2.500

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2.500

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Rmerge0.057
Total number of observations267328

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Number of reflections81628
Completeness [%]72.030

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Redundancy3.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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8.4

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme10 (mg/ml)
101reservoirisopropanol15 (%)
111reservoirPEG300020-24 (%)
121reservoirHEPES0.1 (M)
21drop50 (mM)
31dropbeta-mercaptoethanol0.5 (mM)
41dropEDTA0.5 (mM)
51dropNAD1 (mM)
61dropTris-HCl1.25 (mM)
71dropisopropanol7.5 (%)
81dropPEG300010-12 (%)
91dropHEPES0.05 (M)

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PDB entries from 2024-05-15

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