2HAQ
Crystal Structure of Cyclophilin A from Leishmania Donovani
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 2004-06-08 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 48.590, 48.590, 141.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.930 - 1.970 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.19700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1XO7.PDB |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.930 | 2.020 |
High resolution limit [Å] | 1.970 | 1.970 |
Rmerge | 0.068 | 0.293 |
Number of reflections | 12516 | |
<I/σ(I)> | 30.1 | 4.5 |
Completeness [%] | 99.0 | 86.6 |
Redundancy | 8.1 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.01M TRIS, 7.5% PEG3350, 0.005M IMID 0.02% AZIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE RESERVOIR CONTAINING 40% PEG3350 IN THE SAME BUFFER. PROTEIN CONCENTRATION: 10 MG/ML, temperature 293K |