5YR5
Human methionine aminopeptidase type 1b (F309L mutant) in complex with Ovalicin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2017-03-19 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.392, 77.339, 47.464 |
| Unit cell angles | 90.00, 87.95, 90.00 |
Refinement procedure
| Resolution | 31.240 - 1.600 |
| R-factor | 0.1782 |
| Rwork | 0.177 |
| R-free | 0.20120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gz5 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.726 |
| Data reduction software | DENZO (2.3.1) |
| Data scaling software | SCALEPACK (2.2.0) |
| Phasing software | MOLREP (11.5.05) |
| Refinement software | REFMAC (5.8.0230) |
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 | 0.056 | 0.036 | 0.427 |
| Rmeas | 0.065 | 0.042 | 0.514 |
| Rpim | 0.034 | 0.022 | 0.280 |
| Number of reflections | 45241 | 4615 | 4450 |
| <I/σ(I)> | 17.3 | ||
| Completeness [%] | 99.8 | 99.8 | 98.1 |
| Redundancy | 3.6 | 3.7 | 3.3 |
| CC(1/2) | 0.998 | 0.844 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 298 | 0.1M Bistris pH-6.2, 19% PEG3350, 5% glycerol |
