1OZM
Y106F mutant of Z. mobilis TGT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-05-28 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.390, 64.720, 71.880 |
| Unit cell angles | 90.00, 97.02, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.950 |
| Rwork | 0.184 |
| R-free | 0.19800 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1pud |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.070 * | 0.294 * |
| Total number of observations | 109129 * | |
| Number of reflections | 29077 | |
| Completeness [%] | 96.4 | 94 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 25 * | Romier, C., (1996) Proteins: Struct.,Funct., Genet., 24, 516. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 2 | 1 | reservoir | PEG8000 | 13 (%) | |
| 3 | 1 | reservoir | dithiothreitol | 1 (mM) | |
| 4 | 1 | reservoir | agarose | 0.2 (%) | |
| 5 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
| 6 | 1 | drop | 2 (M) | ||
| 7 | 1 | drop | dithiothreitol | 1 (mM) | |
| 8 | 1 | drop | protein | 12 (mg/ml) |
