1M35
Aminopeptidase P from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-03-25 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.08 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 209.047, 313.963, 162.034 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.400 |
| Rwork | 0.195 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Tetramer of aminopeptidase P from Escherichia coli. Tetramer created from structure of hexagonal form (PDB code 1AZ9) using crystallographic symmetry |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.058 * | 0.300 * |
| Number of reflections | 197708 | |
| <I/σ(I)> | 22.67 | 4.1 |
| Completeness [%] | 95.7 | 87.7 |
| Redundancy | 4.2 * | 3.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | 277 | PEG 4000, Tris.HCl, sodium acetate, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | Tris | 20 (mM) | pH8.5 |
| 3 | 1 | reservoir | PEG4000 | 25 (%) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 5 | 1 | reservoir | sodium acetate | 0.2 (M) | pH8.0 |
| 6 | 1 | reservoir | 10 (mM) |
