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1OK6

Orthorhombic crystal form of an Archaeal fructose 1,6-bisphosphate aldolase

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 21 21 21
Unit cell lengths89.900, 176.500, 185.700
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.390

*

R-factor0.233
Rwork0.232
R-free0.26300
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ojx
RMSD bond length0.013

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RMSD bond angle1.300

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.470
High resolution limit [Å]2.3902.390
Rmerge0.1210.372
Number of reflections106518
<I/σ(I)>13.32.7
Completeness [%]93.669
Redundancy5.43.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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7.5

*

20

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9% (W/V) PEG 4000, 0.1 M NA ACETATE PH 5.0
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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