3E8Z
X-ray structure of rat arginase I-N130A mutant: the unliganded complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F2 |
| Synchrotron site | CHESS |
| Beamline | F2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 32 |
| Unit cell lengths | 87.500, 87.500, 100.110 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.770 - 2.000 |
| R-factor | 0.236 |
| Rwork | 0.236 |
| R-free | 0.28000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rla |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.400 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.077 | 0.260 |
| Number of reflections | 53201 | |
| <I/σ(I)> | 12.3 | 3 |
| Completeness [%] | 91.8 | 66.1 |
| Redundancy | 2.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | drops containing 3 microL of protein solution [5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM BEC, 2 mM MnCl2] and 3 microL of precipitant solution [0.1 M CHES (pH 9.5), 20% PEG 3350, 0.2 M NaCl] were equilibrated over a 1 mL reservoir of precipitant solution., VAPOR DIFFUSION, HANGING DROP |
