4A8R
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, 98.220, 102.070 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 70.770 - 1.420 |
| R-factor | 0.10426 |
| Rwork | 0.103 |
| R-free | 0.12971 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2glk |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.059 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.500 | 1.460 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Rmerge | 0.070 | 0.140 |
| Number of reflections | 168537 | |
| <I/σ(I)> | 52 | 19 |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 42 | 20 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 28.7 MG/ML PROTEIN, 1.4 MG/ML PROTEIN COVALENTLY LABELED WITH A RUTHENIUM-CONTAINING LABEL, 0.9 M AMMONIUM SULPHATE, 100 MM HEPES PH 7.0 |
