4BOB
Structure of Complement regulator-acquiring surface protein 3 (CRASP- 3, ErpP or BBN38) 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 21 21 21 |
| Unit cell lengths | 27.030, 55.130, 81.370 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.740 - 2.530 |
| R-factor | 0.2362 |
| Rwork | 0.235 |
| R-free | 0.26087 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4j38 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.708 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.740 | 2.670 |
| High resolution limit [Å] | 2.530 | 2.530 |
| Rmerge | 0.110 | 0.270 |
| Number of reflections | 3927 | |
| <I/σ(I)> | 6.7 | 3.5 |
| Completeness [%] | 90.5 | 86.8 |
| Redundancy | 2.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 28% PEG 3350, pH 7.5 |
