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1LB3

Structure of recombinant mouse L chain ferritin at 1.2 A resolution

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsLURE BEAMLINE DW32
Synchrotron siteLURE
BeamlineDW32
Temperature [K]150
Detector technologyIMAGE PLATE
Collection date2000-04-17
DetectorMARRESEARCH
Wavelength(s)0.966
Spacegroup nameF 4 3 2
Unit cell lengths180.590, 180.590, 180.590
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution14.000 - 1.210
R-factor0.1335
Rwork0.132
R-free0.16000

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Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1h96
RMSD bond length0.014
RMSD bond angle1.690
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareSHELXL-97
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]14.0001.250
High resolution limit [Å]1.2101.210
Rmerge0.078

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0.602

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Total number of observations399787

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Number of reflections745095144

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<I/σ(I)>6.42
Completeness [%]98.498.4
Redundancy5.54.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.4293

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Granier, T., (2001) Acta Crystallogr., D57, 1491.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein3.5 (mg/ml)
21dropTris20 (mM)pH7.4
31reservoirammonium sulfate0.92 (M)
41reservoir0.4 (%)
51reservoir3 (mM)

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