4A8I
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 | 2011-09-19 |
| Detector | ADSC CCD |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 92.410, 98.140, 102.080 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 70.870 - 0.950 |
| R-factor | 0.12015 |
| Rwork | 0.120 |
| R-free | 0.13226 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2glk |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.136 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 0.970 | 0.970 |
| High resolution limit [Å] | 0.950 | 0.950 |
| Rmerge | 0.050 | 0.430 |
| Number of reflections | 560892 | |
| <I/σ(I)> | 2.6 | 4 |
| Completeness [%] | 99.0 | 96 |
| Redundancy | 4 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 32,7 MG/ML PROTEIN, 0.6 M AMMONIUM SULPHATE, 100 MM HEPES PH 7.0 |
