3LD0
Crystal structure of B.licheniformis Anti-TRAP protein, an antagonist of TRAP-RNA interactions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-01-08 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.87 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 118.544, 99.865, 123.178 |
| Unit cell angles | 90.00, 117.61, 90.00 |
Refinement procedure
| Resolution | 29.270 - 2.200 |
| R-factor | 0.19449 |
| Rwork | 0.194 |
| R-free | 0.25910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bx9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.204 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0008) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.200 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.074 | 0.280 |
| Number of reflections | 128724 | |
| <I/σ(I)> | 11.9 | 4.4 |
| Completeness [%] | 99.8 | 97 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1 M Tris-HCl pH 8.0-8.5 buffer, 0.2 M of MgCl2 salt and 20-25 % of poly(ethylene) glycol 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
