5EG2
SET7/9 N265A in complex with AdoHcy and TAF10 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97903 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 83.198, 83.198, 95.859 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.907 - 1.550 |
| R-factor | 0.1479 |
| Rwork | 0.147 |
| R-free | 0.17120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4j83 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.182 |
| Data reduction software | HKL-2000 (v706) |
| Data scaling software | HKL-2000 (v706) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1.9-1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.590 |
| High resolution limit [Å] | 1.550 | 3.820 | 1.550 |
| Rmerge | 0.068 | 0.037 | 0.904 |
| Rmeas | 0.071 | 0.039 | 0.949 |
| Rpim | 0.022 | 0.012 | 0.289 |
| Total number of observations | 612830 | ||
| Number of reflections | 56195 | ||
| <I/σ(I)> | 19.49 | ||
| Completeness [%] | 100.0 | 99.6 | 100 |
| Redundancy | 10.9 | 9.9 | 10.7 |
| CC(1/2) | 0.999 | 0.906 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.4 | 293 | 1:1 ratio of protein solution to crystallization solution. Protein solution: 4.0-8.0 mg/mL protein, 2.5 mM AdoMet, 2.0 mM TAF10 peptide, and 2.0 mM TCEP Crystallant solution: 0.99 - 1.02 M sodium citrate, 12 - 22 mM nickel (II) chloride, and 100 mM imidazole pH 8.4 |
