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1OK4

Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]100
Collection date2002-02-15
Spacegroup nameP 1 21 1
Unit cell lengths82.400, 157.300, 101.500
Unit cell angles90.00, 108.20, 90.00
Refinement procedure
Resolution40.000

*

- 2.100
R-factor0.164
Rwork0.163
R-free0.18700

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ojx
RMSD bond length0.013
RMSD bond angle1.300

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Refinement softwareREFMAC (5.1.19)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.0002.190
High resolution limit [Å]2.1002.100
Rmerge0.0710.272
Number of reflections125363
<I/σ(I)>13.62.3
Completeness [%]90.259.3
Redundancy3.62.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5

*

20

*

9% (W/V) PEG 4000, 0.1 M NA ACETATE PH 5.0, 1-8% GLYCEROL, 100 MM DHAP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein3 (mg/ml)
21dropHEPES-NaOH10 (mM)pH7.5
31drop100 (mM)
41dropdithiothreitol1 (mM)
51reservoirPEG40009 (%(w/v))
61reservoirsodium acetate0.1 (M)pH5.0

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