2VPL
The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-09-18 |
| Detector | MARRRESEARCH |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 76.100, 144.350, 56.160 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.300 |
| R-factor | 0.212 |
| Rwork | 0.209 |
| R-free | 0.27400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hw8 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.415 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.400 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.120 | 0.420 |
| Number of reflections | 26880 | |
| <I/σ(I)> | 12.9 | 2.6 |
| Completeness [%] | 95.1 | 94.3 |
| Redundancy | 4.4 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
