8J7C
Crystal structure of triosephosphate isomerase from Leishmania orientalis at 1.88A with an arsenic ion bound at Cys57
Replaces: 5CG7Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLRI BEAMLINE BL7.2W |
Synchrotron site | SLRI |
Beamline | BL7.2W |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-05-11 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.5500 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 81.440, 76.450, 94.940 |
Unit cell angles | 90.00, 101.14, 90.00 |
Refinement procedure
Resolution | 19.980 - 1.880 |
R-factor | 0.17366 |
Rwork | 0.171 |
R-free | 0.21377 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.564 |
Data reduction software | MOSFLM (7.0.9) |
Data scaling software | pointless (1.8.8) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.560 | 1.920 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.082 | 0.549 |
Rmeas | 0.101 | 0.682 |
Rpim | 0.059 | 0.399 |
Number of reflections | 46160 | 2463 |
<I/σ(I)> | 11.9 | 2.4 |
Completeness [%] | 98.6 | 81.2 |
Redundancy | 2.8 | 2.6 |
CC(1/2) | 0.991 | 0.598 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.9 | 291.15 | Equal volumes (1.0 microliter) of enzyme (24.2 mg/ml in 50 mM potassium phosphate buffer, pH 8.0, containing 50 mM KCl, 5 mM DTT, and 10% glycerol) and precipitant (PEG8000 18% w/v in 0.2 mM calcium acetate hydrate, 0.1 M and sodium cacodylate trihydrate, pH 5.9) |