Table 1. Data processing and model refinement statistics for the reported crystal structures.
Data sets were collected and processed as described in the online methods section. The dose rate did not exceed 0.01 e−/Å2/s and the mean per-crystal exposure time is given as 〈Texposure〉 for each sample. Except for tau peptide and TGF-βm:TβRII, reflections were integrated to the corners of the detector; the final resolution cutoff was determined based on CC1/2 and the stability of the refinement procedure.
| Tau peptide (PDB id: 5k7n; EMDB id: EMD- 8216) |
Lysozyme (PDB id: 5k7o; EMBD id: EMD-8217) |
TGF-βm:TβRII (PDB id: 5ty4; EMDB id: EMD- 8472) |
Xylanase (PDB id: 5k7p; EMBD id: EMD-8218) |
Thaumatin (PDB id: 5k7q; EMBD id: EMD-8219) |
Trypsin (PDB id: 5k7r; EMBD id: EMD-8220) |
Proteinase K (PDB id: 5k7s; EMBD id: EMD- 8221) |
Thermolysin (PDB id: 5k7t; EMBD id: EMD-8222) |
|
|---|---|---|---|---|---|---|---|---|
| Data collection | ||||||||
| Resolution1 (Å) | 14.70–1.10 | 30.58–1.50 | 26.64–2.90 | 25.55–1.90 | 27.73–2.11 | 27.63–1.50 | 20.75–1.30 | 30.14–1.60 |
| Number of crystals | 2 | 7 | 3 | 4 | 3 | 10 | 6 | 4 |
| 〈Texposure〉 (s) | 159.9 | 127.7 | 140.8 | 172.7 | 179.7 | 155.8 | 122.2 | 187.6 |
| Molecular weight (kDa) |
0.7 | 14.4 | 19.1 | 21.0 | 22.2 | 23.4 | 28.9 | 34.6 |
| Data processing | ||||||||
| Resolution1 (Å) | 14.70–1.10 (1.23–1.10) |
30.59–1.80 (2.06–1.80) |
26.64–2.90 (3.07–2.90) |
25.55–2.30 (2.63–2.30) |
27.73–2.50 (2.86–2.50) |
25.86–1.70 (1.79–1.70) |
20.75–1.60 (1.64–1.60) |
30.14–2.50 (2.75–2.50) |
| Space group | C121 | P43212 | P212121 | P212121 | P41212 | P212121 | P43212 | P6122 |
| Unit cell | ||||||||
| a, b, c (Å) | 29.42, 4.99, 37.17 |
76.10, 76.10, 36.80 |
41.53, 71.33, 79.51 |
49.10, 59.02, 70.00 |
57.78, 57.78, 149.70 |
53.12, 56.08, 64.38 |
67.60, 67.60, 101.36 |
90.75, 90.75, 126.13 |
| α, β, γ (°) | 90, 111.55, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 120 |
| # total reflections1 | 6,185 (463) | 100,693 (282) | 14,911 (2,371) | 38,699 (348) | 51,116 (1,563) | 145,833 (402) | 302,892 (2,044) | 224,846 (314) |
| # unique reflections1 |
3,319 (255) | 14,955 (207) | 3,884 (614) | 10,664 (214) | 12,786 (614) | 23,542 (281) | 46,369 (1,005) | 25,029 (173) |
| CC1/21 | 0.987 (0.639) | 0.901 (0.099) | 0.951 (0.255) | 0.918 (0.201) | 0.848 (0.089) | 0.722 (0.028) | 0.912 (0.056) | 0.847 (0.199) |
| 〈I/σI〉1 | 2.4 (1.1) | 3.7 (1.1) | 3.3 (0.8) | 3.5 (1.2) | 3.5 (2.0) | 2.6 (0.4) | 3.4 (0.9) | 5.6 (3.6) |
| Completeness1 | 83.0 (79.4) | 96.8 (91.8) | 71.9 (71.3) | 82.44 (74.9) | 93.6 (92.2) | 87.5 (56.2) | 96.1 (85.8) | 97.0 (96.8) |
| Multiplicity1 | 1.9 (1.8) | 8.6 (6.1) | 3.8 (3.9) | 4.2 (3.8) | 4.4 (3.9) | 6.9 (3.1) | 8.2 (5.7) | 12.3 (12.2) |
| Refinement | ||||||||
| Rwork1 (%) | 20.97 (21.04) | 23.95 (32.33) | 29.19 (39.51) | 22.95 (35.40) | 25.13 (34.08) | 24.79 (38.72) | 22.35 (36.33) | 28.99 (34.78) |
| Rfree1, 2 (%) | 22.28 (22.43) | 28.42 (37.94) | 32.80 (42.03) | 26.70 (38.95) | 29.45 (38.98) | 28.11 (42.37) | 25.46 (42.25) | 30.96 (36.64) |
| RSCC | 0.84 | 0.89 | 0.72 | 0.85 | 0.86 | 0.89 | 0.91 | 0.86 |
| # residues | 6 | 129 | 166 | 190 | 207 | 223 | 279 | 316 |
| # protein atoms | 53 | 1,001 | 1,327 | 1,481 | 1,551 | 1,629 | 2,029 | 2,432 |
| # water molecules |
2 | 87 | 0 | 23 | 18 | 195 | 221 | 21 |
| # ligand atoms | 0 | 3 | 0 | 2 | 0 | 2 | 2 | 13 |
| 〈ADP〉 (Å2) | ||||||||
| Protein | 12.4 | 13.4 | 47.8 | 25.5 | 20.3 | 13.9 | 8.1 | 4.9 |
| Water | 17.3 | 14.3 | 19.4 | 13.3 | 14.9 | 13.4 | 4.2 | |
| Ligand | 16.7 | 66.5 | 19.6 | 18.9 | 7.5 | |||
| R.m.s.d. bonds (Å) | 0.012 | 0.004 | 0.012 | 0.002 | 0.002 | 0.005 | 0.004 | 0.003 |
| R.ms.d. angles (°) | 0.770 | 0.609 | 1.573 | 0.496 | 0.462 | 0.739 | 0.663 | 0.509 |
| Ramachandran (outliers, favored) (%) |
0.0, 100 | 0.0, 97.6 | 2.5, 89.9 | 0.0, 96.3 | 0.0, 95.1 | 0.0, 96.4 | 0.4, 96.8 | 0.0, 94.9 |
1
Numbers in parentheses reflect the highest resolution shell for either data collection or refinement.
2
In all cases the test set comprises approximately 5% of the unique reflections, where possible chosen to match that of the deposited data for the MR search model.