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1HFO

The Structure of the Macrophage Migration Inhibitory Factor from Trichinella Spiralis.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-3
Synchrotron siteESRF
BeamlineID14-3
Temperature [K]100
Detector technologyCCD
Collection date1999-11-15
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths110.128, 88.344, 86.355
Unit cell angles90.00, 131.13, 90.00
Refinement procedure
Resolution28.330 - 1.650
R-factor0.225
Rwork0.225
R-free0.28100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1mif
RMSD bond length0.008
RMSD bond angle24.900

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.0001.710
High resolution limit [Å]1.6501.650
Rmerge0.057

*

0.281

*

Total number of observations163895

*

Number of reflections729157060

*

<I/σ(I)>3.62.5
Completeness [%]97.697.6
Redundancy2.32.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Batch method

*

4.6CRYSTALS GROWN BY HANGING DROP METHOD. WELL CONTAINED 400-600 AMMONIUM ACETATE, 30-36% PEG4K, 100MM SODIUM ACETATE PH4.6. DROP CONTAINED 1:1 MIX OF WELL AND 16.5MG/ML TSMIF IN MINIMAL BUFFER., pH 4.60
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein16.5 (mg/ml)
211ammonium acetate400-600 (mM)
311PEG400030-36 (%)
411sodium acetate100 (mM)

225946

PDB entries from 2024-10-09

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