Table 1.
Data collection, phasing and refinement statistics
| ATG12~ATG5– ATG16N: crystal Ia |
ATG12~ATG5– ATG16N: crystal IIa |
ATG12~ATG5–ATG16N(I17M L21M I36M L43M)b | |||
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | P212121 | C2 | C2 | ||
| Cell dimensions | |||||
| a, b, c (Å) | 43.8, 113.2, 210.7 | 135.1, 58.9, 90.8 | 102.8, 45.4, 100.7 | ||
| 90, 90, 90 | 90, 129.1, 90 | 90, 102.6, 90 | |||
| Peak | Inflection | Remote | |||
| Wavelength (Å) | 1.0000 | 1.0092 | 0.9796 | 0.9799 | 0.9724 |
| Resolution (Å)c | 50.0–2.7 (2.80–2.70) | 50.0–2.9 (3.00–2.90) | 50.0–2.9 (3.00–2.90) | 50.0–2.9 (3.00–2.90) | 50.0–2.9 (3.00–2.90) |
| Rmergec | 10.0 (63.6) | 5.6 (54.1) | 6.7 (33.5) | 6.1 (34.5) | 6.0 (31.6) |
| I / Ic | 18.5 (2.7) | 22.6 (1.9) | 24.0 (5.3) | 27.9 (5.2) | 17.8 (3.7) |
| Completeness (%)c | 99.9 (100.0) | 98.6 (92.4) | 99.9 (99.4) | 100.0 (99.8) | 99.7 (99.2) |
| Redundancyc | 6.9 (6.1) | 4.4 (3.7) | 7.2 (6.6) | 7.2 (6.5) | 3.6 (3.4) |
| Refinement | |||||
| Resolution (Å) | 44.1–2.7 | 36.2–2.9 | |||
| No. reflections | 29598 | 12465 | |||
| Rwork / Rfree | 17.6 / 23.6 | 21.5 / 25.4 | |||
| No. atoms | |||||
| Protein | 6469 | 3226 | |||
| Ligand/ion | 2 | 1 | |||
| Water | 76 | 0 | |||
| B-factors | |||||
| Protein | 67.5 | 138.8 | |||
| Ligand/ion | 58.9 | 121.6 | |||
| Water | 50.1 | n/a | |||
| R.m.s. deviations | |||||
| Bond lengths (Å) | 0.003 | 0.006 | |||
| Bond angles (°) | 0.66 | 0.51 | |||
a
Native.
b
Selenomethionine.
c
Values in parentheses are for the highest-resolution shell. Each data set was collected from one crystal.