1FXH
MUTANT OF PENICILLIN ACYLASE IMPAIRED IN CATALYSIS WITH PHENYLACETIC ACID IN THE ACTIVE SITE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X31 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-09-25 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.014, 64.084, 64.225 |
| Unit cell angles | 72.92, 73.91, 73.54 |
Refinement procedure
| Resolution | 20.000 - 1.970 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.21500 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.720 * |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.000 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Rmerge | 0.041 | 0.124 |
| Number of reflections | 50404 | |
| <I/σ(I)> | 15.7 | |
| Completeness [%] | 97.3 | 95 |
| Redundancy | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 4 * | drop consists of equal amounts of protein and precipitant solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 8 (mg/ml) | |
| 2 | 1 | reservoir | mPEG2000 | 12-15 (%) | precipitant |
| 3 | 1 | reservoir | MOPS | 50 (mM) | precipitant |
