4AXZ
Borrelia burgdorferi outer surface lipoprotein BBA73
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 |
| Collection date | 2012-02-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 153.630, 47.100, 34.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.150 - 2.090 |
| R-factor | 0.21513 |
| Rwork | 0.214 |
| R-free | 0.24472 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4aly |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.383 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.130 | 2.200 |
| High resolution limit [Å] | 2.080 | 2.090 |
| Rmerge | 0.080 | 0.360 |
| Number of reflections | 15649 | |
| <I/σ(I)> | 6.3 | 2 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 13.8 | 12.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 0.1M HEPES, PH 7.0, 14% PEG 3350, 0.05M NAH2PO4 |
