2FN9
Thermotoga maritima Ribose Binding Protein Unliganded 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 | 2005-07-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.997 |
| Spacegroup name | F 2 2 2 |
| Unit cell lengths | 120.901, 136.826, 144.465 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.400 |
| R-factor | 0.181 |
| Rwork | 0.180 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dri |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.199 |
| 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 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Number of reflections | 115461 | |
| <I/σ(I)> | 1.7 | |
| Completeness [%] | 99.0 | 91.4 |
| Redundancy | 5.8 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.9 | 290 | 0.2M NaCl, 0.1M Bis-Tris pH5.9, 25% PEG 3350, MICRO-BATCH, temperature 290K |
