5BNK
Crystal structure of T75C mutant of Triosephosphate isomerase from Plasmodium falciparum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-20 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.95372 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.360, 76.880, 74.480 |
| Unit cell angles | 90.00, 97.79, 90.00 |
Refinement procedure
| Resolution | 73.790 - 1.800 |
| R-factor | 0.2087 |
| Rwork | 0.206 |
| R-free | 0.25810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1o5x |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.850 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 73.792 | 33.037 | 1.900 |
| High resolution limit [Å] | 1.800 | 5.690 | 1.800 |
| Rmerge | 0.024 | 0.593 | |
| Rmeas | 0.066 | ||
| Rpim | 0.032 | 0.013 | 0.336 |
| Total number of observations | 167317 | 5230 | 24014 |
| Number of reflections | 40771 | ||
| <I/σ(I)> | 12.6 | 28.9 | 2.2 |
| Completeness [%] | 100.0 | 98.6 | 100 |
| Redundancy | 4.1 | 4 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 296 | 16% PEG 1450, 100mM HEPES, 10 mM calcium chloride, 0.5 mM EDTA, 0.5 mM DTT, 0.5 mM sodium azide |
