2A0M
Arginase superfamily protein from Trypanosoma cruzi
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-12-02 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | H 3 |
| Unit cell lengths | 128.875, 128.875, 42.671 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.873 - 1.603 |
| Rwork | 0.168 |
| R-free | 0.19540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | low resolution SAD structure |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.343 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.2.0005 24/04/2001) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 3.450 | 1.600 |
| Rmerge | 0.067 | 0.047 | 0.537 |
| Number of reflections | 32939 | ||
| <I/σ(I)> | 10.952 | 23.582 | 0.997 |
| Completeness [%] | 94.6 | ||
| Redundancy | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 298 | 0.4 ul protein 8.7 mg/ml, 0.4 ul crystallization buffer, 100mM potassium bromide, 42% PEG 1000, 100mM Na citrate, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |






