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1DC6

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 date1999-07-18
DetectorMAC Science DIP-2030
Spacegroup nameC 1 2 1
Unit cell lengths85.450, 134.470, 67.340
Unit cell angles90.00, 107.89, 90.00
Refinement procedure
Resolution20.000 - 2.000
R-factor0.224

*

Rwork0.224
R-free0.29100
RMSD bond length0.010
RMSD bond angle1.421
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.050
High resolution limit [Å]1.9002.010
Rmerge0.0600.317
Total number of observations660366

*

Number of reflections51859
<I/σ(I)>19.6
Completeness [%]91.448.1

*

Redundancy12.733
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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