Table 1.
Summary of diffraction data and structure refinement statistics
| Diffraction data | ||
| Crystal | 23C3-epitope peptide | 23C3-W43A peptide |
| Wavelength (Å) | 1.5418 | 1.5418 |
| Space group | P212121 | P212121 |
| Cell parameters | ||
| a/b/c (Å) | 42.3/92.0/122.5 | 41.7/92.1/122.1 |
| Resolution range (Å) | 20.0–2.80 (2.90–2.80)a | 20.0–2.80 (2.90–2.80) |
| Observed reflections | 82,967 (8415) | 66,404 (6296) |
| Unique reflections [I/σ(I) > 0] | 12,316 (1192) | 12,155 (1171) |
| Average redundancy | 6.7 (7.1) | 5.4 (5.3) |
| Average I/σ(I) | 5.0 (2.1) | 6.3 (3.1) |
| Completeness (%) | 98.4 (98.4) | 99.4 (99.4) |
| Wilson B-factor (Å2) | 58.9 | 55.6 |
| Rmerge (%)b | 13.5 (29.3) | 8.4 (22.9) |
| Statistics of refinement and model | ||
| No. of reflections [Fo > 0σ(Fo)] | ||
| Working set | 11,470 (836) | 11,476 (824) |
| Free R set | 613 (32) | 609 (35) |
| R−factor (%)c | 24.8 (37.3) | 24.1 (31.5) |
| Free R−factor (%) | 29.2 (47.7) | 29.7 (39.5) |
| No. of protein residues | 438 | 436 |
| Fab/Peptide | 429/9 | 429/7 |
| No. of sugar residues | 4 | 4 |
| Average B-factor of all atoms (Å2) | 35.4 | 33.5 |
| Fab/Peptide | 34.8/40.7 | 33.0/33.2 |
| Sugar | 64.2 | 62.1 |
| r.m.s.d. bond lengths (Å) | 0.006 | 0.010 |
| r.m.s.d. bond angles (°) | 1.003 | 1.171 |
| Luzzati atomic positional error (Å) | 0.46 | 0.42 |
| Ramachandran plot (%) | ||
| Most favored regions | 84.9 | 86.8 |
| Allowed regions | 14.0 | 11.4 |
| Generously allowed regions | 0.3 | 1.1 |
| Disallowed regions | 0.8 | 0.8 |
a
Numbers in parentheses refer to the highest-resolution shell.
b
Rmerge = ∑hkl∑i|Ii(hkl)i − 〈I(hkl)〉|/∑hkl∑iIi(hkl).
c
R−factor = ∑hkl ||Fo|−|Fc||/∑hkl |Fo|.