Table S1.
Data collection and structure refinement statistics
| Statistic | XylFII-LytSN-xyl | XXylFII-LytSN-D103A | XylFII | Se-Met* |
| Wavelength, Å | 0.9798 | 0.9798 | 0.9798 | 0.9798 |
| Resolution, Å | 2.2–50.0 | 2.5–50.0 | 2.1–50.0 | 2.6–50.0 |
| Space group | C2221 | P41 21 2 | P1 | C2221 |
| Until cell | ||||
| a, b, c, Å | 105.6, 143.6, 87.1 | 144.9, 144.9, 103.1 | 67.5, 68.1, 76.7 | 105.6, 143.6, 87.1 |
| α, β, γ, ° | 90, 90, 90 | 90, 90, 90 | 89.9, 65.1, 87.3 | 90, 90, 90 |
| Unique reflections | 33,221 (2,748)† | 38,385 (3,768) | 70,577 (6,701) | 20,879 (1,726) |
| Multiplicity | 6.4 | 5.7 | 3.8 | 12.1 |
| I/σ(I) | 14.61 (3.0) | 20.46 (5.1) | 15.8 (7.8) | 32.9 (8.3) |
| Completeness, % | 97.87 (81.9) | 99.73 (100.0) | 96.77 (91.6) | 100 (100) |
| Rwork/Rfree‡ | 0.187/0.215 | 0.229/0.253 | 0.180/0.214 | |
| Number of atoms | 3,320 | 5,144 | 9,153 | |
| Ligand | 10 | 40 | ||
| Water | 231 | 140 | 816 | |
| Protein residues | 397 | 647 | 1,087 | |
| RMS, bonds | 0.008 | 0.011 | 0.011 | |
| Angles | 1.06 | 2.03 | 1.32 | |
| Ramachandran favored, % | 95 | 100 | 97 | |
| Outliers, % | 0 | 0 | 0 | |
| Average B factor | 39.1 | 57.0 | 23.1 | |
| Protein | 38.7 | 57.1 | 22.5 | |
| Ligand | 55.1 | 14.6 | ||
| Water | 43.9 | 55.2 | 30.6 |
*
The Se-Met data were collected from the XylFII-LytSN-xyl form.
†
Numbers in parentheses represent the highest-resolution shell.
‡
R = Σhkl||Fo| − |Fc||/Σhkl|Fo|.