1SCF
HUMAN RECOMBINANT STEM CELL FACTOR
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-07 |
| Detector | FUJI |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.820, 82.550, 88.190 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.24200 |
| Structure solution method | MAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 22.800 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MADLSQ |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.056 * | 0.581 * |
| Number of reflections | 65689 | |
| <I/σ(I)> | 15.3 | 1.6 |
| Completeness [%] | 94.9 | 72 |
| Redundancy | 2.75 | 2.23 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 * | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 38 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 10 (mM) | |
| 3 | 1 | drop | 80 (mM) | ||
| 4 | 1 | reservoir | PEG400 | 25 (%(w/v)) | |
| 5 | 1 | reservoir | 220 (mM) | ||
| 6 | 1 | reservoir | HEPES | 100 (mM) | |
| 7 | 1 | reservoir | dithiothreitol | 5-10 (mM) |
