2GU7
E. coli methionine aminopeptidase unliganded, 1:0.5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-09-01 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.200, 61.980, 77.050 |
| Unit cell angles | 90.00, 107.36, 90.00 |
Refinement procedure
| Resolution | 14.000 - 2.000 |
| R-factor | 0.227 |
| Rwork | 0.208 |
| R-free | 0.24400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xnz |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.274 |
| 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] | 20.000 | 14.310 | 2.110 |
| High resolution limit [Å] | 2.000 | 6.320 | 2.000 |
| Rmerge | 0.050 | 0.024 | 0.235 |
| Total number of observations | 3353 | 16052 | |
| Number of reflections | 31180 | ||
| <I/σ(I)> | 13.1 | 20.2 | 3.3 |
| Completeness [%] | 99.7 | 90.3 | 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 |
