1R2S
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE D03B-MX1 |
| Synchrotron site | LNLS |
| Beamline | D03B-MX1 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-09-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.37 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.229, 80.289, 174.283 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.000 * - 2.850 |
| R-factor | 0.174 * |
| Rwork | 0.172 |
| R-free | 0.21190 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hti |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.358 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.000 * | 2.920 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.124 | 0.264 * |
| Number of reflections | 20064 | |
| <I/σ(I)> | 6.11 | 2.55 |
| Completeness [%] | 80.9 | 58.3 |
| Redundancy | 1.93 | 1.31 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | PEG 4000, MgCl2, 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) |
