Methods development for diffraction and spectroscopy studies of metalloenzymes at X-ray free-electron lasers.
Philos Trans R Soc Lond B Biol Sci
; 369(1647): 20130590, 2014 Jul 17.
Article
em En
| MEDLINE
| ID: mdl-24914169
ABSTRACT
X-ray free-electron lasers (XFELs) open up new possibilities for X-ray crystallographic and spectroscopic studies of radiation-sensitive biological samples under close to physiological conditions. To facilitate these new X-ray sources, tailored experimental methods and data-processing protocols have to be developed. The highly radiation-sensitive photosystem II (PSII) protein complex is a prime target for XFEL experiments aiming to study the mechanism of light-induced water oxidation taking place at a Mn cluster in this complex. We developed a set of tools for the study of PSII at XFELs, including a new liquid jet based on electrofocusing, an energy dispersive von Hamos X-ray emission spectrometer for the hard X-ray range and a high-throughput soft X-ray spectrometer based on a reflection zone plate. While our immediate focus is on PSII, the methods we describe here are applicable to a wide range of metalloenzymes. These experimental developments were complemented by a new software suite, cctbx.xfel. This software suite allows for near-real-time monitoring of the experimental parameters and detector signals and the detailed analysis of the diffraction and spectroscopy data collected by us at the Linac Coherent Light Source, taking into account the specific characteristics of data measured at an XFEL.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Espectrometria por Raios X
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Difração de Raios X
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Software
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Complexo de Proteína do Fotossistema II
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Elétrons
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Lasers
Idioma:
En
Revista:
Philos Trans R Soc Lond B Biol Sci
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos