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Science ; 337(6092): 362-4, 2012 Jul 20.
Artigo em Inglês | MEDLINE | ID: mdl-22653729

RESUMO

Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.


Assuntos
Cristalografia por Raios X/métodos , Conformação Proteica , Animais , Lasers , Muramidase/química , Muramidase/efeitos da radiação
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