1R2R
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-06-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9330 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.550, 75.952, 166.010 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.790 - 1.500 |
| R-factor | 0.1609 * |
| Rwork | 0.159 |
| R-free | 0.18950 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | A partially refined dimer of rabbit muscle TIM structure (crystal form B) |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.393 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.790 * | 1.520 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.067 * | 0.327 |
| Number of reflections | 135276 | |
| <I/σ(I)> | 18.34 | 2.25 |
| Completeness [%] | 88.7 | 65.8 |
| Redundancy | 3.81 | 2.06 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | PEG 4000, MgCl2, DMSO, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG4000 | 24 (%(w/v)) | |
| 2 | 1 | reservoir | 0.2 (M) | ||
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
| 4 | 1 | reservoir | DMSO | 1.1 (M) | |
| 5 | 1 | drop | protein | 10 (mg/ml) |
