7LOX
The structure of Agmatinase from E. Coli at 3.2 A displaying guanidine in the active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-12-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.771 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 129.028, 129.028, 88.290 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 64.510 - 3.200 |
| R-factor | 0.1741 |
| Rwork | 0.172 |
| R-free | 0.21780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3npi |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.400 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.510 | 3.314 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.156 | 0.156 |
| Rmeas | 0.158 | 0.158 |
| Number of reflections | 14314 | 1418 |
| <I/σ(I)> | 26.7 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 39.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | Protein at 12 mg/mL in Buffer 25 mM Tris-HCl pH 8.0, 2 mM MnCl. Crystallization: 0.2 M Lithium sulfate monohydrate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3350 |
