6NEE
Crystal structure of a reconstructed ancestor of Triosephosphate isomerase from eukaryotes
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 103 |
| Detector technology | IMAGE PLATE |
| Collection date | 2016-04-29 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 |
| Unit cell lengths | 43.020, 48.772, 71.205 |
| Unit cell angles | 91.28, 100.14, 118.65 |
Refinement procedure
| Resolution | 38.423 - 1.900 |
| R-factor | 0.1646 |
| Rwork | 0.163 |
| R-free | 0.20170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2i9e |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.960 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_3290: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.472 | 1.968 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.071 | 0.454 |
| Number of reflections | 37060 | 2648 |
| <I/σ(I)> | 12.3 | 3 |
| Completeness [%] | 95.0 | 91.4 |
| Redundancy | 3.9 | 3.9 |
| CC(1/2) | 0.997 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 0.1M HEPS pH 7.5, 20% PEG 8000. Protein concentration 6 mg/mL in 10 mM Triethanolamine pH 7.6, 1 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 mM PGH |
