4CQD
The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-12-14 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.346, 87.063, 113.859 |
| Unit cell angles | 90.00, 104.58, 90.00 |
Refinement procedure
| Resolution | 43.570 - 2.250 |
| R-factor | 0.16768 |
| Rwork | 0.166 |
| R-free | 0.19434 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qt3 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.180 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.300 | 2.370 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.190 | 0.950 |
| Number of reflections | 47468 | |
| <I/σ(I)> | 9 | 3 |
| Completeness [%] | 99.3 | 98.6 |
| Redundancy | 6.7 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.8 | 3.5 MG/ML PROTEIN OVER A RESERVOIR OF 2.5 M MALONATE PH 6.0, 10% (V/V) MALATE/MES/TRIS BUFFER AT PH 7.8; DROPS WERE 150 NL PROTEIN, 120 NL RESERVOIR AND 30 NL SEEDS FROM THE NATIVE CRYSTALS. |
