1OSG
Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-11-18 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.08 |
| Spacegroup name | P 65 |
| Unit cell lengths | 121.633, 121.633, 157.214 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 3.000 |
| R-factor | 0.21992 |
| Rwork | 0.213 |
| R-free | 0.28600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1KXG with the waters removed |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.360 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.081 * | |
| Number of reflections | 26356 | |
| <I/σ(I)> | 10.5 | 2.5 |
| Completeness [%] | 99.6 | 41 * |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 292 | 20% PEG 3350, 1.0 M LiCl, 0.1M sodium cacodylate, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | pH8.0 |
| 3 | 1 | drop | 500 (mM) | ||
| 4 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH6.7 |
| 5 | 1 | reservoir | PEG3350 | 19-21 (%) | |
| 6 | 1 | reservoir | 0.7-1.1 (M) |
