1F32
CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-10-03 |
| Detector | MAC Science DIP-2030B |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 30.455, 72.717, 31.137 |
| Unit cell angles | 90.00, 101.03, 90.00 |
Refinement procedure
| Resolution | 19.580 - 1.750 |
| R-factor | 0.215 * |
| Rwork | 0.211 |
| R-free | 0.25500 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.058 | 0.263 |
| Total number of observations | 42096 * | |
| Number of reflections | 13394 | 726 * |
| <I/σ(I)> | 20.7 | |
| Completeness [%] | 99.6 | 97.4 * |
| Redundancy | 3 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | used seeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | PEG4000 | 25 (%(w/v)) | |
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | spermidine-HCl | 3 (mM) | |
| 5 | 1 | drop | 2-mercaptoethanol | 1 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
| 7 | 1 | reservoir | 2-mercaptoethanol | 2 (mM) |
