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Proc Natl Acad Sci U S A ; 111(48): 17122-7, 2014 Dec 02.
Artigo em Inglês | MEDLINE | ID: mdl-25362050

RESUMO

The emerging method of femtosecond crystallography (FX) may extend the diffraction resolution accessible from small radiation-sensitive crystals and provides a means to determine catalytically accurate structures of acutely radiation-sensitive metalloenzymes. Automated goniometer-based instrumentation developed for use at the Linac Coherent Light Source enabled efficient and flexible FX experiments to be performed on a variety of sample types. In the case of rod-shaped Cpl hydrogenase crystals, only five crystals and about 30 min of beam time were used to obtain the 125 still diffraction patterns used to produce a 1.6-Å resolution electron density map. For smaller crystals, high-density grids were used to increase sample throughput; 930 myoglobin crystals mounted at random orientation inside 32 grids were exposed, demonstrating the utility of this approach. Screening results from cryocooled crystals of ß2-adrenoreceptor and an RNA polymerase II complex indicate the potential to extend the diffraction resolution obtainable from very radiation-sensitive samples beyond that possible with undulator-based synchrotron sources.


Assuntos
Físico-Química/instrumentação , Cristalografia por Raios X/métodos , Conformação Proteica , Proteínas/química , Cristalização , Elétrons , Lasers , Modelos Moleculares , Mioglobina/química , RNA Polimerase II/química , Receptores Adrenérgicos beta 2/química , Reprodutibilidade dos Testes , Síncrotrons , Difração de Raios X/métodos , Raios X
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