1OM6
CRYSTAL STRUCTURE OF A COLD ADAPTED ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18, CO-CRYSTALLIZED WITH 5mM EDTA (2 MONTHS)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-04-04 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.98 |
| Spacegroup name | H 3 |
| Unit cell lengths | 180.500, 180.500, 37.350 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.188 |
| Rwork | 0.185 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g9k |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.620 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.100 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.081 * | 0.167 * |
| Total number of observations | 123884 * | |
| Number of reflections | 30649 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 4 * | Villeret, V., (1997) Protein Sci., 6, 2462. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.0 |
| 3 | 1 | drop | protein | 15 (mg/ml) |
