1QDM
CRYSTAL STRUCTURE OF PROPHYTEPSIN, A ZYMOGEN OF A BARLEY VACUOLAR ASPARTIC PROTEINASE.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F2 |
| Synchrotron site | CHESS |
| Beamline | F2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-01-15 |
| Detector | ADSC QUANTUM 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.000, 160.900, 81.400 |
| Unit cell angles | 90.00, 109.60, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.300 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 26.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.059 | 0.250 |
| Number of reflections | 49301 | |
| <I/σ(I)> | 15.8 | |
| Completeness [%] | 69.5 | 29.6 |
| Redundancy | 3.8 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 293 | 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 | 8 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | 0.1 (M) | ||
| 4 | 1 | reservoir | PEG6000 | 15 (%) | |
| 5 | 1 | reservoir | magnesium acetate | 50 (mM) | |
| 6 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
| 7 | 1 | reservoir | sodium azide | 0.02 (%) |
