8KHM
Crystal structure of human methionine aminopeptidase 12 (MAP12) in the unbound form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-03-17 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.97957 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.398, 81.204, 48.893 |
| Unit cell angles | 90.00, 102.33, 90.00 |
Refinement procedure
| Resolution | 27.670 - 1.390 |
| R-factor | 0.1899 |
| Rwork | 0.189 |
| R-free | 0.20810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.895 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 27.670 | 27.670 | 1.480 |
| High resolution limit [Å] | 1.390 | 4.140 | 1.390 |
| Rmerge | 0.062 | 0.022 | 0.881 |
| Rmeas | 0.073 | 0.025 | 1.023 |
| Number of reflections | 58324 | 2292 | 9301 |
| <I/σ(I)> | 12.83 | ||
| Completeness [%] | 99.3 | ||
| Redundancy | 3.8 | ||
| CC(1/2) | 0.999 | 0.999 | 0.765 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 287 | 0.1M HEPES pH 7.2, 0.1M Carboxylic acids, 17% (v/v) MPD, 17% (w/v) PEG 1000, 17% (w/v) PEG 3350 |






