4LOA
X-ray structure of the de-novo design amidase at the resolution 1.8A, Northeast Structural Genomics Consortium (NESG) Target OR398
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 |
| Unit cell lengths | 34.485, 44.335, 57.515 |
| Unit cell angles | 71.07, 75.97, 86.86 |
Refinement procedure
| Resolution | 33.445 - 1.819 |
| R-factor | 0.205 |
| Rwork | 0.203 |
| R-free | 0.24200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1via |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.953 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | BALBES |
| Refinement software | PHENIX (dev_1269) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 33.500 |
| High resolution limit [Å] | 1.800 |
| Rmerge | 0.049 |
| Number of reflections | 27069 |
| <I/σ(I)> | 12.5 |
| Completeness [%] | 96.5 |
| Redundancy | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 277 | Protein solution - 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5), Reservoir solution - 100mM HEPES, 42% PEG 200, microbatch under oil, temperature 277K |
