7LO0
Structure of human ASF1a in complex with a TLK2 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-08-17 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97920 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 88.023, 136.681, 101.316 |
| Unit cell angles | 90.00, 103.22, 90.00 |
Refinement procedure
| Resolution | 98.630 - 2.710 |
| R-factor | 0.2137 |
| Rwork | 0.213 |
| R-free | 0.22560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2i32 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.512 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.2) |
| Refinement software | PHENIX (1.19) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 98.630 | 98.630 | 2.780 |
| High resolution limit [Å] | 2.710 | 12.120 | 2.710 |
| Rmerge | 0.057 | 0.024 | 0.439 |
| Rmeas | 0.068 | 0.028 | 0.530 |
| Rpim | 0.037 | 0.015 | 0.292 |
| Total number of observations | 199527 | 2460 | 13402 |
| Number of reflections | 62051 | 721 | 4441 |
| <I/σ(I)> | 10.9 | 27.2 | 2 |
| Completeness [%] | 98.0 | 96.3 | 96.1 |
| Redundancy | 3.2 | 3.4 | 3 |
| CC(1/2) | 0.998 | 0.998 | 0.863 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 18% PEG3350, 0.2 M of trisodium citrate, pH 5.6 and 2% Octyl-D-glucose |
