7LOL
The structure of Agmatinase from E. Coli at 1.8 A displaying urea and agmatine
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) | 1.0332 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 81.746, 81.746, 207.436 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.790 - 1.800 |
| R-factor | 0.1713 |
| Rwork | 0.170 |
| R-free | 0.19470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3npi |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.354 |
| 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] | 35.790 | 1.864 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.066 | 0.892 |
| Rmeas | 0.068 | 0.916 |
| Number of reflections | 25154 | 2475 |
| <I/σ(I)> | 28.76 | 3.61 |
| Completeness [%] | 99.9 | |
| Redundancy | 19.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 291 | Agmatinase at 12 mg/mL in Buffer 25 mM Tris-HCl pH 8.0, 2 mM MnCl2. Condition: 0.1 M phosphate/citrate pH 4.2 and 40% PEG 300 |
