Table 1.
Statistics of structure determination of four segments of IAPP which form steric zippers.
| 13-ANFLVH-18 | 16-LVHSSN-21 | 22-NFGAILS-28 | 23-FGAILSS-29 | |
|---|---|---|---|---|
| Crystal Parameters | ||||
| Space Group | P21 | P21 | P1 | P1 |
| Cell Dimensions | ||||
| a, b, c (Å) | 4.83, 39.73, 9.87 | 9.64, 9.61, 19.03 | 8.7, 11.6, 21.6 | 8.77, 9.5, 24.74 |
| α, β, γ (°) | 90, 103.69, 90 | 90, 101.22, 90 | 86.4, 82.2, 76.4 | 88.22, 80.00, 70.34 |
| Molecules in Asymmetric Unit | 1 | 1 | 2 | 2 |
| Data collection | ||||
| Synchrotron beamline | APS (24-ID-E) | APS (24-ID-E) | APS (24-ID-E) | APS (24-ID-E) |
| Wavelength (Å) | 0.9792 | 0.9792 | 0.9792 | 0.9792 |
| Resolution (Å) | 1.61 | 1.66 | 1.24 | 1.78 |
| Unique Reflections | 433 | 391 | 2227 | 647 |
| Overall Redundancy | 3.1 (3.2) | 3.0(3.0) | 2.9(2.6) | 5.2(4.0) |
| Completeness (%) | 93.8(87.0) | 90.6(97.1) | 97.8(96.9) | 93.4(72.3) |
| Rmerge (%)b | 14.7(13.3) | 7.6(14.9) | 16.6(55.8) | 24.1(69.6) |
| <I/σI> | 6.6(9.7) | 14.1(9.1) | 6.5(1.6) | 4.3(1.4) |
| Refinement | ||||
| Resolution (Å) | 19.86-1.61 | 19.53-1.66 | 21.34-1.24 | 24.35-1.78 |
| Rwork(%)c | 11.2 | 16.7 | 17.3 | 16.7 |
| Rfree(%)d | 16.1 | 19.8 | 20.6 | 21.8 |
| No. atoms | ||||
| Protein | 50 | 46 | 102 | 98 |
| Ligand/ion | 0 | 0 | 0 | 0 |
| Water | 0 | 1 | 7 | 0 |
| Overall B-factors | 7.8 | 4.6 (4.4e) | 2.3(1.9e) | 23.7 |
| R.m.s. deviation | ||||
| Bond length (Å) | 0.003 | 0.004 | 0.008 | 0.016 |
| Bond angle (°) | 0.70 | 1.0 | 1.0 | 2.0 |
a. Values in parentheses correspond to the highest resolution shell.
b
Rmerge=Σ|I–<I>|/ΣI.
c
Rwork=Σ|Fo –Fc |/ΣFo.
d
Rfree= Σ | Fo – Fc | / Σ Fo, calculated using a random set containing 10% reflections that were not included throughout structure refinement.
e
without water