2EIS
X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from Thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-02 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 3 |
Unit cell lengths | 105.675, 105.675, 105.675 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.260 - 2.100 |
R-factor | 0.219 |
Rwork | 0.219 |
R-free | 0.23900 |
Structure solution method | MAD and MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.080 | 0.287 |
Number of reflections | 23244 | |
<I/σ(I)> | 11.3 | |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 298 | 30% v/v Propylene Glycol, 4% v/v PEG 400, 20% v/v Glycerol, 0.1M Na3Citrate, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |