3FW0
Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL) bound to alpha-hydroxyhippuric acid (non-peptidic substrate)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-09 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.00724 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.930, 75.080, 97.026 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 59.340 - 2.520 |
| R-factor | 0.20939 |
| Rwork | 0.207 |
| R-free | 0.26019 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PALcc native being deposited at the same time as this structure |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.246 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.340 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 13347 | |
| <I/σ(I)> | 23.5 | 2.7 |
| Completeness [%] | 99.6 | 98.9 |
| Redundancy | 6.8 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293 | 0.1M sodium acetate pH=4.8, 0.5mM mercury(II) acetate - 0.2ml mother liquor in reservoir. Then, crystals soaked in 5mM hydroxyhippuric acid for several hours, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
