1LNS
Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-03-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9376 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 92.500, 102.500, 101.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.200 |
| Rwork | 0.184 |
| R-free | 0.22300 |
| Structure solution method | MIR |
| RMSD bond length | 0.006 |
| RMSD bond angle | 24.400 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | MLPHARE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 * | 2.340 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.057 * | 0.170 * |
| Total number of observations | 153738 * | |
| Number of reflections | 46073 * | |
| Completeness [%] | 95.8 * | 95.3 * |
| Redundancy | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 18 * | Chich, J.F., (1995) Proteins., 23. 278. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH8.0 |
| 3 | 1 | drop | 0.1 (M) | ||
| 4 | 1 | drop | glycerol | 10 (%) | |
| 5 | 1 | reservoir | MES | 50 (mM) | pH5.0 |
| 6 | 1 | reservoir | PEG4000 | 7 (%) |
