1EI5
CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-10-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 82.860, 82.860, 204.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 12.500 - 1.900 |
| Rwork | 0.163 |
| R-free | 0.19200 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.031 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.890 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.052 * | 0.346 |
| Number of reflections | 62212 | |
| <I/σ(I)> | 14.6 | |
| Completeness [%] | 93.2 * | 81 |
| Redundancy | 7.9 * | 4.76 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 21 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | dithiothreitol | 10 (mM) | |
| 4 | 1 | drop | EDTA | 0.1 (mM) | |
| 5 | 1 | drop | sodium azide | 1 (mM) | |
| 6 | 1 | reservoir | PEG400 | 30 (%) | |
| 7 | 1 | reservoir | sodium acetate | 0.1 (M) |
