Crystal structure data collection and refinement statistics
| Criteria | Cross-linked SHD-Kar3Vik1 |
| Space group | P212121 |
| Cell dimensions | |
| a, b, c (Å) | 88.1, 94.9, 114.6 |
| α, β, γ (°) | 90, 90, 90 |
| Wavelength | 0.979206 |
| Resolution (Å)a | 25–2.3 (2.34–2.3) |
| Rmergea | 5.1 (60.1) |
| I/σIa | 19.7 (3.2) |
| Completeness (%)a | 99.9 (99.8) |
| Redundancya | 8.6 (6.2) |
| Resolution (Å)a | 25–2.3 (2.34–2.3) |
| No. reflectionsb | 40710 (2701) |
| Rwork/Rfreec | 0.21/0.24 |
| No. atoms | |
| Protein | 5361 |
| Water | 246 |
| Average B-factors (Å2) | |
| Protein | 69.991 |
| Water | 54.972 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 0.891 |
| PDB accession no. | 4ETP |
| Criteria | Cross-linked SHD-Kar3Vik1 |
| Space group | P212121 |
| 88.1, 94.9, 114.6 | |
| α, β, γ (°) | 90, 90, 90 |
| Wavelength | 0.979206 |
| Resolution (Å) | 25–2.3 (2.34–2.3) |
| Rmerge | 5.1 (60.1) |
| 19.7 (3.2) | |
| Completeness (%) | 99.9 (99.8) |
| Redundancy | 8.6 (6.2) |
| Resolution (Å) | 25–2.3 (2.34–2.3) |
| No. reflections | 40710 (2701) |
| 0.21/0.24 | |
| Protein | 5361 |
| Water | 246 |
| Protein | 69.991 |
| Water | 54.972 |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 0.891 |
| PDB accession no. |
Data in parentheses represent the highest resolution shell.
Data in parentheses represent the number of reflections used for the calculation of Rfree.
Rfactor = ∑|Fobs−Fcalc| / ∑|Fobs|.
Where Rwork refers to the Rfactor for the data utilized in the refinement and Rfree refers to the Rfactor for 5% of the data that were excluded from the refinement.
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