1HI9
Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-10-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8445,1.2832,1.2834 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 145.110, 165.860, 109.930 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.400 |
| R-factor | 0.232 |
| Rwork | 0.232 |
| R-free | 0.26800 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.240 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.490 |
| High resolution limit [Å] | 2.403 | 2.400 |
| Rmerge | 0.055 * | 0.247 * |
| Total number of observations | 438502 * | |
| Number of reflections | 51831 | |
| <I/σ(I)> | 11.7 | 3.7 |
| Completeness [%] | 96.9 | 98.6 |
| Redundancy | 3.48 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | 18% PEG6000, 100MM TRIS, PH 8.5, 5MM NACL, 5MM MGCL2 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 18 (mg/ml) | |
| 2 | 1 | drop | Tris | 10 (mM) | |
| 3 | 1 | drop | 5 (mM) | ||
| 4 | 1 | reservoir | PEG6000 | 18 (%(w/v)) | |
| 5 | 1 | reservoir | Tris | 100 (mM) | |
| 6 | 1 | reservoir | 5 (mM) | ||
| 7 | 1 | reservoir | 5 (mM) | ||
| 8 | 1 | reservoir | 5 (mM) |
