| 000 | 01469 a2200373 4500 | ||
|---|---|---|---|
| 005 | 20250517024650.0 | ||
| 264 | 0 | _c20160108 | |
| 008 | 201601s 0 0 eng d | ||
| 022 | _a1399-0047 | ||
| 024 | 7 |
_a10.1107/S1399004715001674 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aLangkilde, Annette E | |
| 245 | 0 | 0 |
_aThe architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy. _h[electronic resource] |
| 260 |
_bActa crystallographica. Section D, Biological crystallography _cApr 2015 |
||
| 300 |
_a882-95 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAmyloid _xchemistry |
| 650 | 0 | 4 | _aMicroscopy, Electron |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 |
_aPeptide Termination Factors _xchemistry |
| 650 | 0 | 4 |
_aPrions _xchemistry |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aSaccharomyces cerevisiae _xchemistry |
| 650 | 0 | 4 |
_aSaccharomyces cerevisiae Proteins _xchemistry |
| 650 | 0 | 4 | _aScattering, Small Angle |
| 650 | 0 | 4 | _aX-Ray Diffraction |
| 700 | 1 | _aMorris, Kyle L | |
| 700 | 1 | _aSerpell, Louise C | |
| 700 | 1 | _aSvergun, Dmitri I | |
| 700 | 1 | _aVestergaard, Bente | |
| 773 | 0 |
_tActa crystallographica. Section D, Biological crystallography _gvol. 71 _gno. Pt 4 _gp. 882-95 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1107/S1399004715001674 _zAvailable from publisher's website |
| 999 |
_c24780911 _d24780911 |
||