9ME8
Co-crystal structure of maltose binding protein (MBP)-human SENP3 fusion protein in complex with PELP1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2024-10-25 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.9202 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 140.970, 140.970, 119.633 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.710 - 2.930 |
| R-factor | 0.2035 |
| Rwork | 0.202 |
| R-free | 0.23220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.752 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.710 | 2.980 |
| High resolution limit [Å] | 2.930 | 2.930 |
| Rmerge | 0.296 | 3.518 |
| Rmeas | 0.310 | 3.673 |
| Rpim | 0.091 | 1.051 |
| Number of reflections | 28983 | 1468 |
| <I/σ(I)> | 8.6 | 1.1 |
| Completeness [%] | 96.6 | 100 |
| Redundancy | 11.4 | 12.1 |
| CC(1/2) | 0.994 | 0.350 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 0.085M HEPES pH 7.5, 17-20% (v/v) PEG8000 |
