1N69
Crystal structure of human saposin B
Experimental procedure
| Experimental method | MAD, SE-MET |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F2 |
| Synchrotron site | CHESS |
| Beamline | F2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-04-21 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9789, 0.9793 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 72.140, 72.140, 94.366 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 * - 2.200 |
| R-factor | 0.222 |
| Rwork | 0.222 |
| R-free | 0.26200 |
| Structure solution method | MAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.200 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SnB |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.059 * | 0.289 * |
| Number of reflections | 14644 | |
| <I/σ(I)> | 9 | 2.6 |
| Completeness [%] | 98.3 | 98.3 |
| Redundancy | 10.5 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 295 | Ahn, V.E., (2003) Protein Expression Purif., 27, 186. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 30 (mg/ml) | |
| 2 | 1 | reservoir | PEG3350 | 16 (%) | |
| 3 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH5.8 |
