Crystallization of the crenarchaeal SRP core.
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.
Rosendal
Ken R
KR
Biochemie-Zentrum (BZH), University of Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Sinning
Irmgard
I
Wild
Klemens
K
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D019641:DNA, Archaeal / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D019642:RNA, Archaeal / Q000737:chemistry; D018271:Signal Recognition Particle / Q000737:chemistry* / Q000235:genetics; D016944:Sulfolobus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D019843:Archaeal Proteins; D019641:DNA, Archaeal; D019642:RNA, Archaeal; D018271:Signal Recognition Particle