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 |