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1GVF

Structure of tagatose-1,6-bisphosphate aldolase

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyCCD
DetectorMAR, RAXIS
Wavelength(s)1.282,1.283,1.127,1.030, 1.5418,0.933
Spacegroup nameI 2 2 2
Unit cell lengths72.650, 100.460, 206.660
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 1.450
R-factor0.17

*

R-free0.13000

*

Structure solution methodDIRECT METHODS
RMSD bond length0.018
RMSD bond angle0.030

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareRSPS
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]29.8001.480
High resolution limit [Å]1.4501.450
Rmerge0.0640.292
Total number of observations1086028

*

Number of reflections131455

*

<I/σ(I)>151.5
Completeness [%]98.497.9
Redundancy33
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5

*

20

*

pH 6.40
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropenzyme6.5 (mg/ml)
21dropTris-HCl50 (mM)pH7.5
31dropPGH20 (mM)
41reservoirethylene glycol7-12 (%(v/v))
51reservoir10 (mM)
61reservoirsodium cacodylate42 (mM)pH6.4

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PDB entries from 2024-05-15

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