1SKF
CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 293 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.593, 54.528, 108.697 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.186 * |
| Rwork | 0.183 |
| R-free | 0.24100 * |
| Structure solution method | MIRAS |
| RMSD bond length | 0.015 * |
| RMSD bond angle | 3.000 * |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 38.400 |
| High resolution limit [Å] | 1.750 |
| Rmerge | 0.099 * |
| Number of reflections | 23085 |
| Completeness [%] | 80.0 |
| Redundancy | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.2 | 20 * | pH 7.20 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 1.3 (mg/ml) | |
| 10 | 1 | reservoir | dithiothreitol | 0.2 (mM) | |
| 11 | 1 | reservoir | PEG4000 | 15 (%(w/v)) | can be replaced by PEG8000 |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | 0.4 (M) | ||
| 4 | 1 | drop | 10 (mM) | ||
| 5 | 1 | drop | dithiothreitol | 0.2 (mM) | |
| 6 | 1 | drop | PEG4000 | 7.5 (%(w/v)) | can be replaced by PEG8000 |
| 7 | 1 | reservoir | Tris-HCl | 50 (mM) | |
| 8 | 1 | reservoir | 0.4 (M) | ||
| 9 | 1 | reservoir | 10 (mM) |
