Table 2.
Data collection and refinement statistics
| LSD1-8a + CoREST complex with H3 inhibitor peptidea | |
|---|---|
| Space group | I222 |
| Unit cell (Å) | a = 119.7 |
| b = 181.2 | |
| c = 233.4 | |
| Resolution (Å) | 3.0 |
| Rsymbc (%) | 11.3 (49.7) |
| Completenessc (%) | 98.9 (99.8) |
| Unique reflections | 50,357 |
| Redundancy | 4.1 (4.1) |
| I/σc | 10.2 (2.1) |
| Rcrystd (%) | 20.7 |
| Rfreed (%) | 24.9 |
| RMS bond length (Å) | 0.017 |
| RMS bond angles (°) | 1.81 |
aThe final model consists of residues 171-836 of LSD1-8a (including residues Asp-Thr-Val-Lys corresponding to exon 8a, which are inserted after Ala369 and are named 369A-369B-369C-369D), a FAD molecule, residues 308-440 of CoREST, and residues 1-16 of the Lys4Met peptide.
bRsym = Σ|Ii − <I>|/ΣIi, where Ii is the intensity of ith observation and <I> is the mean intensity of the reflection.
cValues in parentheses are for reflections in the highest resolution shell.
dRcryst = Σ| Fobs − Fcalc|/Σ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively. The set of reflections used for Rfree calculations and excluded from refinement was extracted from the structure factor file relative to the Protein Data Bank entry 2IW5.