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1DC4

STRUCTURAL ANALYSIS OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA COLI: DIRECT EVIDENCE FOR SUBSTRATE BINDING AND COFACTOR-INDUCED CONFORMATIONAL CHANGES

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsENRAF-NONIUS FR571
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-08-03
DetectorMAC Science DIP-2030
Spacegroup nameI 41
Unit cell lengths120.820, 120.820, 157.680
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.500
R-factor0.198
Rwork0.198
R-free0.25800
RMSD bond length0.008

*

RMSD bond angle1.380

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.540
High resolution limit [Å]2.5002.500
Rmerge0.0580.216
Total number of observations299063

*

Number of reflections38926
<I/σ(I)>22.6
Completeness [%]99.899.9

*

Redundancy7.685.36
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.6

*

18

*

PEG 4000, MAGNESIUM CHLORIDE, TRIS, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropTris-HCl20 (mM)
21drop200 (mM)
31dropdithiothreitol1 (mM)
41dropEDTA1 (mM)
51dropprotain20 (mg/ml)
61reservoirPEG400015 (%)
71reservoir0.8-0.9 (M)
81reservoirTris-HCl0.1 (M)

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