5AKQ
X-ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC
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 | 2014-04-03 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.204, 86.581, 114.066 |
| Unit cell angles | 90.00, 104.36, 90.00 |
Refinement procedure
| Resolution | 110.500 - 2.600 |
| R-factor | 0.20637 |
| Rwork | 0.205 |
| R-free | 0.24129 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cqb |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.722 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.200 | 2.720 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.260 | 1.040 |
| Number of reflections | 30950 | |
| <I/σ(I)> | 6.9 | 2.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.3 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 4.0 MG/ML PROTEIN; RESERVOIR WAS 2.56 M MALONATE AT PH 7.0; DROPS WERE 200 NL PLUS 200 NL |
