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1QMO

Structure of FRIL, a legume lectin that delays hematopoietic progenitor maturation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7A
Temperature [K]287
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Spacegroup nameP 65 2 2
Unit cell lengths151.360, 151.360, 309.880
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 3.500
R-factor0.232
Rwork0.232
R-free0.25200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)MODEL
RMSD bond length0.008
RMSD bond angle26.900

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS (0.4)
Refinement softwareCNS (0.4)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0003.620
High resolution limit [Å]3.5003.500
Rmerge0.159

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Total number of observations257389

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Number of reflections26919

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<I/σ(I)>11.34.8
Completeness [%]99.4
Redundancy12.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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6.5METHOD 'HANING DROP BOTTOM', 20 % PEG 8000, 0.1 M NACACODYLATE, PH 6.5, 0.2 M (NH4)2SO4, WITH A 5 MICROLITER PROTEIN SOLUTION DROP, (4.3 MG/ML)+ 5 MICROLITER BOTTOM SOLUTION + 1 MICROLITER TRIMANNOSIDE SOLUTION (90 MM)
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein4.3 (mg/ml)
21dropMan(alpha1-3)[Man(alpha1-6)]Man(alpha1-O-Me)90 (mM)
31dropbottom solution
41reservoirPEG800011 (%)bottom solution
51reservoirNa cacodylate0.1 (M)bottom solution
61reservoirammonium sulfate0.2 (M)bottom solution

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PDB entries from 2024-05-01

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