4A8N
Protein crystallization and microgravity: glucose isomerase crystals grown during the PCDF-PROTEIN mission
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM16 |
Synchrotron site | ESRF |
Beamline | BM16 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-19 |
Detector | ADSC CCD |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 92.530, 98.070, 102.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.770 - 1.200 |
R-factor | 0.11089 |
Rwork | 0.110 |
R-free | 0.12788 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2glk |
RMSD bond length | 0.025 |
RMSD bond angle | 2.078 |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 1.230 | 1.230 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.060 | 0.160 |
Number of reflections | 280608 | |
<I/σ(I)> | 26 | 7 |
Completeness [%] | 99.0 | 99 |
Redundancy | 5 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 28.7 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 |