8CRG
E. coli adenylate kinase in complex with two ADP molecules as a result of enzymatic AP4A hydrolysis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-07-09 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.976254 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.810, 77.360, 59.600 |
| Unit cell angles | 90.00, 95.48, 90.00 |
Refinement procedure
| Resolution | 37.610 - 1.490 |
| R-factor | 0.1639 |
| Rwork | 0.163 |
| R-free | 0.19070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.297 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP (11.0) |
| Refinement software | REFMAC (5.0.32) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.610 | 1.530 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.034 | 0.868 |
| Rmeas | 0.043 | 1.085 |
| Rpim | 0.023 | 0.542 |
| Number of reflections | 285900 | 21040 |
| <I/σ(I)> | 15.31 | 1.53 |
| Completeness [%] | 99.2 | 98.9 |
| Redundancy | 3.4 | 3.4 |
| CC(1/2) | 0.999 | 0.515 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291.15 | 20 % (w/v) PEG 3350, 100 mM Bis-tris propane pH 6.5 |
