5MMD
TMB-1. Structural insights into TMB-1 and the role of residue 119 and 228 in substrate and inhibitor binding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-05-11 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.918409 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 71.398, 127.195, 44.274 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.287 - 1.750 |
R-factor | 0.1951 |
Rwork | 0.192 |
R-free | 0.24790 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.319 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.082 | 0.492 |
Number of reflections | 38067 | |
<I/σ(I)> | 10.8 | 1.7 |
Completeness [%] | 91.9 | 59.25 |
Redundancy | 3.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 0.10 M HEPES pH 8.0, 4.75% glycerol 32% polyethylene glycol (PEG) monomethyl ether (MME) 2k. |