6M00
crystal structure of Methionine aminopeptidase from Pyrococcus furiosus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2020-01-09 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 62 |
| Unit cell lengths | 137.684, 137.684, 61.332 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.790 - 3.200 |
| R-factor | 0.2441 |
| Rwork | 0.242 |
| R-free | 0.27640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wkm |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.880 |
| Data reduction software | DENZO (2.3.1) |
| Data scaling software | SCALEPACK (2.2.0) |
| Phasing software | MOLREP (11.4.03) |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.860 | 45.860 | 3.000 |
| High resolution limit [Å] | 2.850 | 9.010 | 2.850 |
| Rmerge | 0.181 | 0.042 | 1.732 |
| Rmeas | 0.196 | 0.044 | 1.959 |
| Rpim | 0.074 | 0.015 | 0.886 |
| Total number of observations | 3317 | 7199 | |
| Number of reflections | 14342 | 452 | 1732 |
| <I/σ(I)> | 6.7 | 20.2 | 0.8 |
| Completeness [%] | 92.7 | 90.3 | 76.9 |
| Redundancy | 6 | 7.3 | 4.2 |
| CC(1/2) | 0.992 | 0.999 | 0.291 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 0.1 M sodium acetate, 2M NaCl , 5% glycerol |
