1G5Z
CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE PROTEIN C (OSPC) FROM BORRELIA BURGDORFERI STRAIN N40
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-11-23 |
| Detector | MACSCIENCE |
| Wavelength(s) | 1.54078 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 32.079, 47.052, 110.607 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.500* |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.26200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.240 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.067 * | 0.207 * |
| Number of reflections | 5757 | |
| <I/σ(I)> | 14.2 | |
| Completeness [%] | 93.7 | 89.6 |
| Redundancy | 3.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | PEG 1500, EDTA, DTT, Tris, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 10 (mM) | |
| 3 | 1 | reservoir | dithiothreitol | 5 (mM) | |
| 4 | 1 | reservoir | PEG1500 | 12 (%) |
