4BEB
MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP
Replaces: 2Y3TExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH MX-555 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 127.112, 123.112, 160.110 |
| Unit cell angles | 90.00, 111.48, 90.00 |
Refinement procedure
| Resolution | 19.885 - 2.989 |
| R-factor | 0.2555 |
| Rwork | 0.255 |
| R-free | 0.29650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w00 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.999 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP (IN AUTO-RICKSHAW PACKAGE) |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.170 |
| High resolution limit [Å] | 2.989 | 2.989 |
| Rmerge | 0.120 | 0.400 |
| Number of reflections | 92081 | |
| <I/σ(I)> | 10.7 | 3.7 |
| Completeness [%] | 98.8 | 96.2 |
| Redundancy | 4.2 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 6UL PROTEIN MIXED WITH 0.8UL OF 2M NH4F AND 2UL WELL SOLUTION OF 22% W/V PEG4K, 0.1M MES PH 5.7. 20C, SITTING DROP |
