Extending X-ray crystallography to allow the imaging of noncrystalline materials, cells, and single protein complexes.
Annu Rev Phys Chem
; 59: 387-410, 2008.
Article
em En
| MEDLINE
| ID: mdl-18031219
ABSTRACT
In 1999, researchers extended X-ray crystallography to allow the imaging of noncrystalline specimens by measuring the X-ray diffraction pattern of a noncrystalline specimen and then directly phasing it using the oversampling method with iterative algorithms. Since then, the field has evolved moving in three important directions. The first is the 3D structural determination of noncrystalline materials, which includes the localization of the defects and strain field inside nanocrystals, and quantitative 3D imaging of disordered materials such as nanoparticles and biomaterials. The second is the 3D imaging of frozen-hydrated whole cells at a resolution of 10 nm or better. A main thrust is to localize specific multiprotein complexes inside cells. The third is the potential of imaging single large protein complexes using extremely intense and ultrashort X-ray pulses. In this article, we review the principles of this methodology, summarize recent developments in each of the three directions, and illustrate a few examples.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Nanoestruturas
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Estados Unidos