1F05
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 103 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-02-06 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.570, 113.570, 69.190 |
| Unit cell angles | 90.00, 101.37, 90.00 |
Refinement procedure
| Resolution | 19.900 - 2.450 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.25800 |
| Starting model (for MR) | 1onr Escherichia coli Transaldolase B |
| RMSD bond length | 0.006 |
| RMSD bond angle | 20.600 * |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.970 | 2.570 |
| High resolution limit [Å] | 2.440 | 2.440 |
| Rmerge | 0.080 * | 0.206 * |
| Total number of observations | 60447 * | |
| Number of reflections | 22520 | |
| <I/σ(I)> | 7.4 | |
| Completeness [%] | 88.2 | 79.7 |
| Redundancy | 2.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 293 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (M) | |
| 3 | 1 | reservoir | PEG4000 | 27 (%(w/v)) | |
| 4 | 1 | reservoir | 0.08 (%) | ||
| 5 | 1 | reservoir | 0.3 (M) |
