1ESI
R248L MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE D41A |
| Synchrotron site | LURE |
| Beamline | D41A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-10-21 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.010, 51.750, 84.080 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.23300 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.900 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA) |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 22.190 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.069 | 0.205 |
| Number of reflections | 21066 | |
| <I/σ(I)> | 8.3 | |
| Completeness [%] | 98.8 | 84.1 |
| Redundancy | 3.8 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 293 | This particular structure is not described in this paper. * |
