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Updated: Aug 29, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Crystallization of the crenarchaeal SRP core
Ken R Rosendal1, Irmgard Sinning, Klemens Wild
1Biochemie-Zentrum (BZH), University of Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Abstract:
Protein translocation across or targeting to membranes mediated by the signal recognition particle (SRP) is a universal mechanism conserved in all domains of life. SRP54 from the crenarchaeon Sulfolobus solfataricus has been recombinantly expressed and crystallized with and without SRP RNA helix 8. The RNA has been transcribed in vitro using ribozyme technology. Both crystal forms are perfect merohedral twins. While SRP54 alone is hemihedrally twinned, the crystals of the SRP54-helix 8 complex indicate tetartohedral twinning, which has not previously been observed in protein crystals. The tetartohedral twinning is enabled by a special diamond-like packing in a trigonal crystal.
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