1LTM
ACCELERATED X-RAY STRUCTURE ELUCIDATION OF A 36 KDA MURAMIDASE/TRANSGLYCOSYLASE USING WARP
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 1995-04-08 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.329, 67.883, 98.853 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| R-factor | 0.189 * |
| Rwork | 0.186 |
| R-free | 0.22100 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.009 |
| RMSD bond angle | 22.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.600 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.050 | 0.261 |
| Total number of observations | 206582 * | |
| Number of reflections | 41653 | |
| <I/σ(I)> | 24.4 | 3.5 |
| Completeness [%] | 94.4 | 91.8 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 * | 295 * | ROD-SHAPED CRYSTALS WERE GROWN AT 295 K IN 1 DAY TO 1 WEEK BY EQUILIBRATING A HANGING DROP, THAT CONSISTED OF 3 UL OF PROTEIN SOLUTION AND 3 UL OF RESERVOIR SOLUTION OF 100 MM BICINE-NAOH, PH 7.8-8.5 AND 0-6% PEG 20K., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7.0 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | isopropanol | 1 (%) | |
| 4 | 1 | drop | PMSF | 1 (mM) | |
| 5 | 1 | reservoir | Bicine-NaOH | 100 (mM) | |
| 6 | 1 | reservoir | PEG20000 | 0-6 (%) |
