2YN7
Crystal structure of an outer surface protein BBA66 from Borrelia burgdorferi
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 | 2012-07-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.910, 51.120, 58.880 |
| Unit cell angles | 90.34, 96.21, 94.40 |
Refinement procedure
| Resolution | 29.780 - 2.250 |
| R-factor | 0.19032 |
| Rwork | 0.188 |
| R-free | 0.23232 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4axz |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.540 |
| 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] | 33.010 | 2.360 |
| High resolution limit [Å] | 2.240 | 2.240 |
| Rmerge | 0.060 | 0.290 |
| Number of reflections | 21363 | |
| <I/σ(I)> | 9.7 | 2.2 |
| Completeness [%] | 94.3 | 85.2 |
| Redundancy | 1.9 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 18% PEG 2000 MME, 0.1 M TRIS PH 9.0 |
