5A2U
Crystal structure of BBA68 or BbCRASP-1 from Borrelia burgdorferi strain B31
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 54.630, 54.630, 394.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.450 - 3.300 |
| R-factor | 0.24795 |
| Rwork | 0.246 |
| R-free | 0.28643 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w33 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.998 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.330 | 3.480 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.040 | 0.160 |
| Number of reflections | 9488 | |
| <I/σ(I)> | 9.9 | 3.3 |
| Completeness [%] | 96.9 | 98.5 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 10% PEG 10 000 0.1M TRIS PH 8.0 |
