7S7M
Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66D/T98G/P131S/Q153N) with matrix metalloproteinase-3 catalytic domain (MMP-3cd)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2019-06-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.999995 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 69.280, 69.280, 318.980 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.630 - 3.000 |
| R-factor | 0.2047 |
| Rwork | 0.202 |
| R-free | 0.24840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uea |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.980 |
| Data reduction software | iMOSFLM (7.2.2) |
| Data scaling software | Aimless (0.7.2) |
| Phasing software | MOLREP (11.7.01) |
| Refinement software | PHENIX (1.15rc3_3435) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 15.630 | 15.630 | 3.110 |
| High resolution limit [Å] | 3.000 | 6.330 | 3.000 |
| Rmerge | 0.125 | 0.049 | 0.772 |
| Rmeas | 0.152 | 0.056 | 0.915 |
| Rpim | 0.084 | 0.027 | 0.485 |
| Number of reflections | 9900 | 1684 | 1665 |
| <I/σ(I)> | 6.7 | 16.3 | 1.2 |
| Completeness [%] | 94.7 | 99.7 | 99.64 |
| Redundancy | 3.1 | 4.1 | 3.4 |
| CC(1/2) | 0.943 | 0.998 | 0.469 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 310 | 0.1 M ammonium acetate, 0.1 M Bis-Tris-HCl, pH 5.5, 17% w/v PEG10000 |
