Room temperature structures beyond 1.5 Å by serial femtosecond crystallography

About 2.5 × 10(6) snapshots on microcrystals of photoactive yellow protein (PYP) from a recent serial femtosecond crystallographic (SFX) experiment were reanalyzed to maximum resolution. The resolution is pushed to 1.46 Å, and a PYP structural model is refined at that resolution. The result is compa...

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Detalles Bibliográficos
Autores principales: Schmidt, Marius, Pande, Kanupriya, Basu, Shibom, Tenboer, Jason
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Crystallographic Association 2015
Materias:
SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711625/
https://www.ncbi.nlm.nih.gov/pubmed/26798807
http://dx.doi.org/10.1063/1.4919903
Descripción
Sumario:About 2.5 × 10(6) snapshots on microcrystals of photoactive yellow protein (PYP) from a recent serial femtosecond crystallographic (SFX) experiment were reanalyzed to maximum resolution. The resolution is pushed to 1.46 Å, and a PYP structural model is refined at that resolution. The result is compared to other PYP models determined at atomic resolution around 1 Å and better at the synchrotron. By comparing subtleties such as individual isotropic temperature factors and hydrogen bond lengths, we were able to assess the quality of the SFX data at that resolution. We also show that the determination of anisotropic temperature factor ellipsoids starts to become feasible with the SFX data at resolutions better than 1.5 Å.

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