3T2D
Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, FBP-bound form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 90 |
| Detector technology | PIXEL |
| Collection date | 2010-08-01 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 112.291, 112.291, 151.348 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 54.780 - 1.360 |
| R-factor | 0.10475 |
| Rwork | 0.104 |
| R-free | 0.12590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3t2b |
| RMSD bond length | 0.031 |
| RMSD bond angle | 2.365 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.780 | 1.390 |
| High resolution limit [Å] | 1.360 | 1.360 |
| Rmerge | 0.073 | 0.424 |
| Number of reflections | 102981 | |
| <I/σ(I)> | 18.5 | 5.1 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 9.2 | 8.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | 8% PEG3350, 0.1 M HEPES/NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
