Room temperature structures beyond 1.5 Å by serial femtosecond crystallography

Structural Dynamics
Marius SchmidtJason Tenboer

Abstract

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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Citations

Mar 6, 2016·Archives of Biochemistry and Biophysics·Christopher O BarnesGuillermo Calero
Jun 1, 2016·Lab on a Chip·Shuo SuiSarah L Perry
Nov 13, 2015·Optics Express·Oleksandr YefanovAnton Barty

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Methods Mentioned

BETA
X-ray
electron microscopy

Software Mentioned

REFMAC5
CHEETAH
CrystFEL
PYP
MOLEMAN
COOT

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