Table 1.
MicroED structures of Proteinase K determined from plasma beam milled lamellaea
| Argon milled crystals | Xenon milled crystals | Nitrogen milled crystals | Oxygen milled crystals | Best merge | |
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | P 43 21 2 | P 43 21 2 | P 43 21 2 | P 43 21 2 | P 43 21 2 |
| Cell dimensions | |||||
| a, b, c (Å) | 67.02, 67.02, 107.53 | 67.05, 67.05, 107.02 | 67.12, 67.12, 106.87 | 67.26, 67.26, 106.81 | 67.02, 67.02, 107.53 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 1.4 (1.45–1.4) | 1.45 (1.50–1.45) | 1.8 (1.86–1.8) | 1.5 (1.55–1.5) | 1.39 (1.44–1.39) |
| Rmerge | 0.3235 (1.784) | 0.2942 (1.475) | 0.5183 (1.798) | 0.759 (1.674) | 0.3396 (1.773) |
| <I / σI> | 7.61 (1.40) | 7.73 (1.62) | 4.18 (1.24) | 4.91 (1.03) | 10.78 (1.68) |
| Completeness (%) | 97.27 (96.17) | 98.61 (98.29) | 99.68 (99.21) | 96.20 (95.51) | 99.44 (97.05) |
| Redundancy | 25.8 (20.7) | 21.3 (15.5) | 15.2 (15.0) | 13.7 (11.0) | 54.8 (31.3) |
| Refinement | |||||
| Resolution (Å) | 1.4 | 1.45 | 1.8 | 1.5 | 1.39 |
| No. reflections | 47,738 | 43,468 | 23,288 | 38,542 | 49,781 |
| Rwork / Rfree | 0.1374/0.1735 | 0.1387/0.1770 | 0.1679/0.2121 | 0.1634/0.2138 | 0.1252 / 0.1630 |
| No. atoms | |||||
| Protein | 2063 | 2052 | 2031 | 2047 | 2090 |
| Ligand/ion | 10 | 10 | 2 | 10 | 10 |
| Water | 307 | 294 | 237 | 344 | 284 |
| B-factors | 14.47 | 15.14 | 19.42 | 12.16 | 13.67 |
| Protein | 12.51 | 13.43 | 18.47 | 10 | 12.00 |
| Ligand/ion | 27.44 | 25.25 | 20.14 | 24.69 | 16.38 |
| Water | 27.21 | 26.76 | 27.49 | 24.63 | 25.92 |
| R.m.s. deviations | |||||
| Bond lengths (Å) | 0.015 | 0.009 | 0.004 | 0.002 | 0.014 |
| Bond angles (°) | 1.1 | 0.88 | 0.63 | 0.48 | 1.20 |
aStructures were derived from 5 crystals for argon and xenon, 4 for oxygen and nitrogen, and 12 for the best merge.