2FN8
Thermotoga maritima Ribose Binding Protein Ribose Bound Form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97944 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 72.070, 98.242, 131.099 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.150 |
| R-factor | 0.194 |
| Rwork | 0.193 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dri |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.246 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 25783 | |
| <I/σ(I)> | 25.7 | 3.6 |
| Completeness [%] | 80.9 | 21 |
| Redundancy | 5.8 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6 | 290 | 0.1M RbCl, 0.1M MES pH6.0, 20% PEG 8,000, Micro-Batch, temperature 290K |
