2GTX
Structural Basis of Catalysis by Mononuclear Methionine Aminopeptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-09-04 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.809, 64.257, 76.172 |
| Unit cell angles | 90.00, 108.09, 90.00 |
Refinement procedure
| Resolution | 14.965 - 2.000 |
| R-factor | 0.204 |
| Rwork | 0.196 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xnz |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.277 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 14.965 | 15.360 | 2.110 |
| High resolution limit [Å] | 2.000 | 6.320 | 2.000 |
| Rmerge | 0.077 | 0.027 | 0.254 |
| Total number of observations | 3349 | 15854 | |
| Number of reflections | 30975 | ||
| <I/σ(I)> | 9.5 | 20.9 | 3 |
| Completeness [%] | 99.8 | 92.3 | 100 |
| Redundancy | 3.6 | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 15% PEG 20000, 0.1 M MES (pH 6.5) , VAPOR DIFFUSION, HANGING DROP, temperature 291K |






