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1LK7

Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
DetectorADSC QUANTUM 4
Wavelength(s)0.9326
Spacegroup nameP 21 21 21
Unit cell lengths73.689, 114.923, 119.578
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 2.000
R-factor0.2045
Rwork0.202
R-free0.27000

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1lk5
RMSD bond length0.006

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RMSD bond angle1.320

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Data reduction softwareDENZO
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.000

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2.030
High resolution limit [Å]2.0002.000
Rmerge0.050

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0.387

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Number of reflections67418
Completeness [%]96.3

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96.2

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Redundancy4.0

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3.9

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Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8

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20

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0.1M acetate buffer, 2.0M NaCl, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21dropTris-HCl50 (mM)pH8.0
31drop150 (mM)
41reservoirsodium acetate0.1 (M)pH4.6
51reservoir2.0 (M)

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PDB entries from 2024-10-16

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