6L2B
Crystal structure of cyclophilin mutant I164M from Leishmania donovani at 2.65 angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 2019-04-30 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5406 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 48.618, 48.618, 141.322 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.970 - 2.650 |
Rwork | 0.177 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2haq |
RMSD bond length | 0.002 |
RMSD bond angle | 0.510 |
Data reduction software | CrystalClear (2.0) |
Data scaling software | CrystalClear (2.0) |
Phasing software | CrystalClear (2.0) |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.970 | 2.746 |
High resolution limit [Å] | 2.650 | 2.651 |
Rmerge | 0.102 | 0.102 |
Rmeas | 0.112 | |
Number of reflections | 5381 | 5384 |
<I/σ(I)> | 10.3 | |
Completeness [%] | 99.8 | 99.9 |
Redundancy | 5.58 | 5.58 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | 20mM Tris HCl, 100mM NaCl, 0.02% sodium azide, PEG 3350 (Reservoir 30% and precipitant 3% in the final drop), protein at concentration 5 mg/ml. |