1M22
X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-07-12 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.179, 62.596, 101.906 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 * - 1.400 |
| R-factor | 0.189 * |
| Rwork | 0.188 |
| R-free | 0.19900 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.371 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MLPHARE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 79.000 | 1.490 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.103 | 0.169 |
| Number of reflections | 182206 | |
| <I/σ(I)> | 7.8 | 5.1 |
| Completeness [%] | 99.3 | 95 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 | 289 | Neumann, S., (2002) Acta Crystallogr., Sect.D, 58, 333. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG6000 | 13 (%) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
| 3 | 1 | reservoir | glycerine | 20 (%) | |
| 4 | 1 | reservoir | sodium azide | 0.02 (%) | |
| 5 | 1 | drop | protein | 24 (mg/ml) |
