1RTQ
The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-04-01 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 109.936, 109.936, 91.369 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.000 * - 0.950 |
| R-factor | 0.135 |
| Rwork | 0.135 |
| R-free | 0.15100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 * |
| RMSD bond angle | 0.030 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 0.980 |
| High resolution limit [Å] | 0.950 | 0.950 |
| Rmerge | 0.064 * | 0.230 * |
| Total number of observations | 3348266 * | |
| Number of reflections | 191127 | |
| Completeness [%] | 95.0 | 59 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Schalk, C., (1992) Arch. Biochem. Biophys., 294, 91. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 16 (mg/ml) | |
| 10 | 1 | reservoir | bromophenol blue | 0.02 (%(w/v)) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | 0.4 (M) | ||
| 5 | 1 | reservoir | Tris base | 25 (mM) | |
| 6 | 1 | reservoir | glycine | 160 (mM) | |
| 7 | 1 | reservoir | SDS | 0.8 (%(w/v)) | |
| 8 | 1 | reservoir | 2-mercaptoethanol | 65 (%(v/v)) | |
| 9 | 1 | reservoir | glycerol | 6.5 (%(v/v)) |
