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4A8N

Protein crystallization and microgravity: glucose isomerase crystals grown during the PCDF-PROTEIN mission

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM16
Synchrotron siteESRF
BeamlineBM16
Temperature [K]100
Detector technologyCCD
Collection date2009-09-19
DetectorADSC CCD
Spacegroup nameI 2 2 2
Unit cell lengths92.530, 98.070, 102.050
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution70.770 - 1.200
R-factor0.11089
Rwork0.110
R-free0.12788
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2glk
RMSD bond length0.025
RMSD bond angle2.078
Data reduction softwareXDS
Data scaling softwareXDS
Refinement softwareREFMAC (5.5.0110)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]1.2301.230
High resolution limit [Å]1.2001.200
Rmerge0.0600.160
Number of reflections280608
<I/σ(I)>267
Completeness [%]99.099
Redundancy53.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1728.7 MG/ML PROTEIN, 1.4 MG/ML PROTEIN COVALENTLY LABELED WITH BIS(2,2'-BIPYRIDINE)-4,4'-DICARBOXY BIPYRIDINE-RUTHENIUM DI(N-SUCCINIMIDYL ESTER) BIS(HEXAFLUOROPHOSPHATE), 0.9M AMMONIUM SULPHATE, 100MM HEPES PH 7.0

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