2FS2
Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon
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 | 2003-06-07 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9798 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 69.847, 69.847, 117.168 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.880 - 2.000 |
| Rwork | 0.187 |
| R-free | 0.23000 |
| Structure solution method | SAD |
| RMSD bond length | 0.031 |
| RMSD bond angle | 2.329 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE (2.03) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.093 | 0.462 |
| Number of reflections | 40460 | 3829 |
| <I/σ(I)> | 6.9 | 1.4 |
| Completeness [%] | 93.5 | 88.9 |
| Redundancy | 2.5 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 291 | 13% PEG 4000, 0.1M BIS-TRIS, 20% MPD, 0.2M LITHIUM SULFATE, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
