1MEN
complex structure of human GAR Tfase and substrate beta-GAR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-08-04 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.1 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 147.825, 147.825, 188.036 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.000 * - 2.230 |
| Rwork | 0.220 |
| R-free | 0.26700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mej |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.450 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.000 * | 2.300 |
| High resolution limit [Å] | 2.230 | 2.230 |
| Rmerge | 0.076 | 0.510 |
| Total number of observations | 144600 * | |
| Number of reflections | 38266 * | |
| <I/σ(I)> | 24.3 | 2.54 |
| Completeness [%] | 98.5 * | 86.4 |
| Redundancy | 3.78 * | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 4 * | PEG4000, PEG400, NaCl, Tris pH 8.5, 2mM beta-GAR, VAPOR DIFFUSION, SITTING DROP, temperature 282K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 18-21 (%) | |
| 3 | 1 | reservoir | PEG400 | 2 (%) | |
| 4 | 1 | reservoir | 0.1 (M) | ||
| 5 | 1 | reservoir | Tris | 0.1 (M) | pH8.5 |
