1E3A
A slow processing precursor penicillin acylase from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.710, 64.270, 72.000 |
| Unit cell angles | 66.14, 74.18, 74.23 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.149 |
| Rwork | 0.158 |
| R-free | 0.19700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pnk |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 0.026 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.063 | 0.216 |
| Total number of observations | 133678 * | |
| Number of reflections | 70642 | |
| <I/σ(I)> | 10.3 | 3.16 |
| Completeness [%] | 96.9 | 89.1 |
| Redundancy | 1.9 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.2 | 18 * | 50MM MOPS PH7.2, 18-20% PEG 5KME, 10MM CACL2, pH 7.20 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7.5 (mg/ml) | |
| 2 | 1 | reservoir | MOPS | 50 (mM) | pH7.2 |
| 3 | 1 | reservoir | PEG MME5000 | 18-22 (%(v/v)) | |
| 4 | 1 | reservoir | 10 (mM) |
