Statistics of X-ray diffraction data and structure refinement
| Protein . | αIIbβ3 headpiece native-1 (1mM Mg2+) . | αIIbβ3 headpiece native-2 (5mM Mg2+) . | αIIbβ3 headpiece with RUC-1 (1mM Mg2+) . |
|---|---|---|---|
| Space group | P21212 | P21212 | P21212 |
| Unit cell (a, b, c), Å | 259.0, 144.5, 104.2 | 260.7, 145.2, 104.4 | 259.5, 144.3, 104.4 |
| α, β, γ, ° | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Wavelength, Å | 1.00695 | 0.97948 | 1.00795 |
| Resolution, Å | 50-2.3/2.36-2.30¶ | 50-2.25/2.37-2.25¶ | 50-2.4/2.46-2.40¶ |
| No. of reflections, total/unique | 948 770/169 848 | 1 244 812/187 671 | 807 082/145 845 |
| Completeness, % | 97.7/96.9¶ | 99.9/99.9¶ | 95.1/95.6¶ |
| I/σ(I) | 11.7/2.1¶ | 12.1/1.9¶ | 13.3/2.3¶ |
| Rmerge, %* | 10.0/83.9¶ | 9.4/99.4¶ | 8.9/99.1¶ |
| Rwork†/Rfree‡ | 0.177/0.213 | 0.172/0.213 | 0.172/0.216 |
| RMSD: Bond, Å | 0.007 | 0.009 | 0.007 |
| RMSD: Angle, ° | 1.08 | 1.15 | 1.09 |
| Ramachandran plot§ | 97.0%/2.9%/0.1% | 95.3%/4.4%/0.3% | 95.8%/4.0%/0.2% |
| Molecules/asymmetric unit | 2 | 2 | 2 |
| Resides, αIIb/β3 | 1-454(453)/1-466(471)** | 1-457(453)/1-466(471)** | 1-454(453)/1-466(467)** |
| Non-H atoms, protein/carbohydrate/water | 20770/238/1061 | 20776/180/1227 | 20764/193/792 |
| Protein Data Bank code | 3NID | 3NIG | 3NIF |
| Protein . | αIIbβ3 headpiece native-1 (1mM Mg2+) . | αIIbβ3 headpiece native-2 (5mM Mg2+) . | αIIbβ3 headpiece with RUC-1 (1mM Mg2+) . |
|---|---|---|---|
| Space group | P21212 | P21212 | P21212 |
| Unit cell (a, b, c), Å | 259.0, 144.5, 104.2 | 260.7, 145.2, 104.4 | 259.5, 144.3, 104.4 |
| α, β, γ, ° | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Wavelength, Å | 1.00695 | 0.97948 | 1.00795 |
| Resolution, Å | 50-2.3/2.36-2.30¶ | 50-2.25/2.37-2.25¶ | 50-2.4/2.46-2.40¶ |
| No. of reflections, total/unique | 948 770/169 848 | 1 244 812/187 671 | 807 082/145 845 |
| Completeness, % | 97.7/96.9¶ | 99.9/99.9¶ | 95.1/95.6¶ |
| I/σ(I) | 11.7/2.1¶ | 12.1/1.9¶ | 13.3/2.3¶ |
| Rmerge, %* | 10.0/83.9¶ | 9.4/99.4¶ | 8.9/99.1¶ |
| Rwork†/Rfree‡ | 0.177/0.213 | 0.172/0.213 | 0.172/0.216 |
| RMSD: Bond, Å | 0.007 | 0.009 | 0.007 |
| RMSD: Angle, ° | 1.08 | 1.15 | 1.09 |
| Ramachandran plot§ | 97.0%/2.9%/0.1% | 95.3%/4.4%/0.3% | 95.8%/4.0%/0.2% |
| Molecules/asymmetric unit | 2 | 2 | 2 |
| Resides, αIIb/β3 | 1-454(453)/1-466(471)** | 1-457(453)/1-466(471)** | 1-454(453)/1-466(467)** |
| Non-H atoms, protein/carbohydrate/water | 20770/238/1061 | 20776/180/1227 | 20764/193/792 |
| Protein Data Bank code | 3NID | 3NIG | 3NIF |
Rmerge = ΣhΣi|Ii(h) −<I(h)>|/ΣhΣi|Ii(h)|, where Ii(h) and <I(h)> are the ith and mean measurement of the intensity of reflection h.
Rwork = Σh||Fobs(h)| − |Fcalc(h)||/Σh|Fobs(h)|, where Fobs(h) and Fcalc(h) are the observed and calculated structure factors, respectively. No I/σ cutoff was applied.
Rfree is the R value obtained for a test set of reflections consisting of a randomly selected 0.6% subset of data excluded from refinement.
Residues in favorable, allowed, and outlier of the Ramachandran plot as reported by MOLPROBITY.45
Numbers correspond to the last resolution shell.
Numbers in parentheses correspond to chains C and D.