1YJG
Variable Small Protein 1 of Borrelia turicatae (VspA or Vsp1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 175.857, 34.213, 99.386 |
| Unit cell angles | 90.00, 112.68, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.220 |
| R-factor | 0.20875 |
| Rwork | 0.206 |
| R-free | 0.26486 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Partially refined model for VspA 34-214 derived by molecular replacement starting from Borrelia burgdorferi OspC strain B31 (PDB ID 1GGQ) |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.258 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.220 |
| Rmerge | 0.050 | 0.166 |
| Number of reflections | 26408 | |
| <I/σ(I)> | 26 | 3.4 |
| Completeness [%] | 95.7 | 84.5 |
| Redundancy | 2.93 | 2.68 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 294 | 25% (w/v) PEG 4000, 0.1 M LiCl, and 0.1 mM taurine, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
