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 |