6ELA
Crystal structure of MMP12 in complex with inhibitor BE4.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 2 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-30 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.976254 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.190, 63.320, 78.320 |
Unit cell angles | 90.00, 103.73, 90.00 |
Refinement procedure
Resolution | 38.041 - 1.485 |
R-factor | 0.1732 |
Rwork | 0.171 |
R-free | 0.20670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5i4o |
RMSD bond length | 0.005 |
RMSD bond angle | 0.795 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.440 | 1.570 |
High resolution limit [Å] | 1.480 | 1.480 |
Rmeas | 0.137 | 0.850 |
Number of reflections | 100074 | 15656 |
<I/σ(I)> | 7.85 | 1.68 |
Completeness [%] | 99.4 | 96.4 |
Redundancy | 6.67 | 6.51 |
CC(1/2) | 0.997 | 0.874 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | protein solution: hMMP12 at 314 micro-M + 10 milli-M acetohydroxamate + 1 milli-M BE4, 10% DMSO precipitant: 38% PEG 4K, 0.16 M imidazole piperidine,15% Dioxane, pH 8.5. Cryoprotectant: 40% CM15 (12.5 % diethylene glycol + 12.5 % ethylene glycol + 12.5 % MPD + 12.5 % glycerol + 12.5 % 1,2-propanediol + 12.5 % 1,4-dioxane + 12.5 mM NDSB 201), 25% PEG 6K, 100 milli-M TRIS HCl, pH 7.0 |