3Q1T
Crystal structure of enoyl-coA hydratase from Mycobacterium avium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-18 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97946 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 124.920, 136.890, 104.380 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.350 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.22730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1wz8 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.409 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.410 |
High resolution limit [Å] | 2.350 | 10.510 | 2.350 |
Rmerge | 0.068 | 0.018 | 0.520 |
Number of reflections | 74741 | ||
<I/σ(I)> | 16.58 | 49.58 | 2.82 |
Completeness [%] | 99.4 | 96.1 | 99.9 |
Redundancy | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | MyavA00829eA1 3C protease cleaved PW28936 at 23.9 mg/mL against JCSG+ screen condition H3, 0.1 M BisTris pH 5.5, 25% PEG 3350 with 25% ethylene glycol as cryo-protectant, crystal tracking ID 216914h3., VAPOR DIFFUSION, SITTING DROP |