4D53
Outer surface protein BB0689 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 | 2013-06-27 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 65 |
| Unit cell lengths | 92.210, 92.210, 96.130 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.270 - 1.850 |
| R-factor | 0.18015 |
| Rwork | 0.178 |
| R-free | 0.21581 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.974 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.300 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.030 | 0.190 |
| Number of reflections | 39106 | |
| <I/σ(I)> | 14.4 | 3.8 |
| Completeness [%] | 99.1 | 96.6 |
| Redundancy | 4.3 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 2.0 M AMMONIUM SULFATE, 0.1 M TRIS-HCL PH 8.5 |
