tetano
Editor, Senior Moderator
Acta Crystallogr F Struct Biol Commun. 2014 Feb 1;70(Pt 2):248-51. doi: 10.1107/S2053230X14000430. Epub 2014 Jan 22.
Expression, purification, crystallization and preliminary X-ray analysis of full-length human RIG-I.
Kwok J1, Hui KP2, Lescar J3, Kotaka M1.
Author information
Abstract
The human innate immune system can detect invasion by microbial pathogens through pattern-recognition receptors that recognize structurally conserved pathogen-associated molecular patterns. Retinoic acid-inducible gene I (RIG-I)-like helicases (RLHs) are one of the two major families of pattern-recognition receptors that can detect viral RNA. RIG-I, belonging to the RLH family, is capable of recognizing intracellular viral RNA from RNA viruses, including influenza virus and Ebola virus. Here, full-length human RIG-I (hRIG-I) was cloned in Escherichia coli and expressed in a recombinant form with a His-SUMO tag. The protein was purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.85 ? resolution; the crystal belonged to space group F23, with unit-cell parameters a = b = c = 216.43 ?, α = β = γ = 90?.
KEYWORDS:
human RIG-I
PMID:
24637767
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24637767
Expression, purification, crystallization and preliminary X-ray analysis of full-length human RIG-I.
Kwok J1, Hui KP2, Lescar J3, Kotaka M1.
Author information
Abstract
The human innate immune system can detect invasion by microbial pathogens through pattern-recognition receptors that recognize structurally conserved pathogen-associated molecular patterns. Retinoic acid-inducible gene I (RIG-I)-like helicases (RLHs) are one of the two major families of pattern-recognition receptors that can detect viral RNA. RIG-I, belonging to the RLH family, is capable of recognizing intracellular viral RNA from RNA viruses, including influenza virus and Ebola virus. Here, full-length human RIG-I (hRIG-I) was cloned in Escherichia coli and expressed in a recombinant form with a His-SUMO tag. The protein was purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.85 ? resolution; the crystal belonged to space group F23, with unit-cell parameters a = b = c = 216.43 ?, α = β = γ = 90?.
KEYWORDS:
human RIG-I
PMID:
24637767
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24637767