Table III.
Summary of the TVMV Protease Crystallographic Data
| Parameter | TVMV |
|---|---|
| Data collection | |
| Space group | P212121 |
| Unit cell dimensions | |
| a, b, c (Å) | 76.5, 77.6, 78.5 |
| α, β, γ (°) | 90, 90, 90 |
| Protein molecules/A.U. | 2 |
| Wavelength (Å) | 0.97939 |
| Data processing | |
| Resolution range (Å)a | 35–1.7 (1.76–1.70) |
| No. of reflections | 50064 |
| Rmergea | 0.08 (0.431) |
| I/σIa | 17.4 (2.7) |
| Completeness (%)a | 96.1 (92.7) |
| Redundancya | 5.2 (3.4) |
| Refinement statistics | |
| Resolution range (Å) | 35–1.7 |
| Rwork/Rfree (%) | 17.5/21.0 |
| No. atoms/molecules | |
| Protein | 3591 |
| Water | 553 |
| Formic acid | 1 |
| Average B-factor (Å2) | |
| Protein | 17.4 |
| Water | 32.3 |
| Formic acid | 36.5 |
| R.m.s deviations | |
| Bond lengths (Å) | 0.01 |
| Bond angles (°) | 1.33 |
| Ramachandran plot statistics | |
| Residues in most favored regions | 351 |
| Residues in additional allowed regions | 38 |
| Residues in generously allowed regions | 1 |
| Residues in disallowed regions | 0 |
A.U., asymmetric unit.
a
Values in parentheses refer to the highest resolution shell.