4ZV1
An ancestral arginine-binding protein bound to arginine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-10-17 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.460, 60.410, 103.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.560 - 1.520 |
| R-factor | 0.17154 |
| Rwork | 0.170 |
| R-free | 0.20050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wdn |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.318 |
| Data reduction software | MOSFLM (7.0.9) |
| Data scaling software | Aimless (0.1.29) |
| Phasing software | PHASER (2.5.2) |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.560 | 1.550 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.093 | 0.612 |
| Number of reflections | 40887 | |
| <I/σ(I)> | 12 | 2.4 |
| Completeness [%] | 99.6 | 94.4 |
| Redundancy | 6.9 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 0.2 M Li2SO4, 0.1 M HEPES pH 7.5, 27.5% (w/v) PEG 3350 |
