1ES4
C98N 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] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-06 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.044, 53.739, 107.958 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.900 |
R-factor | 0.179 |
Rwork | 0.179 |
R-free | 0.22500 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 22.690 | 1.930 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.061 | 0.182 |
Number of reflections | 20385 | 1634 * |
<I/σ(I)> | 8.74 | |
Completeness [%] | 89.8 | 95.6 |
Redundancy | 3.9 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 20 * | Tris 0.1M, PEG 6K 30%, NaCl 0.4M, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.3-20 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | ||
3 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
4 | 1 | reservoir | 0.5 (M) |