4K3L
E. coli sliding clamp in complex with AcLF dipeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-04 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.845, 67.464, 81.369 |
| Unit cell angles | 90.00, 113.73, 90.00 |
Refinement procedure
| Resolution | 27.060 - 1.500 |
| R-factor | 0.2191 |
| Rwork | 0.217 |
| R-free | 0.25490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mmi |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.120 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 3.230 | 1.500 |
| Rmerge | 0.058 | 0.030 | 0.919 |
| Number of reflections | 125264 | ||
| <I/σ(I)> | 8.9 | ||
| Completeness [%] | 99.0 | 90.1 | 100 |
| Redundancy | 7.2 | 6.4 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 285 | 100mM MES, 100-150mM CaCl2, 25-30%(v/v) PEG400, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K |
