Crystallization and preliminary X-ray crystallographic analysis of human RGS10 complexed with Gαi3

Hyung Ki Lee, Kyung Hee Rhee, Chan Wha Kim, Kwang Yeon Hwang, Eunice Eun Kyeong Kim

Research output: Contribution to journalArticlepeer-review


G-protein-coupled receptors, which are major targets for drug discovery, play a major role in diverse physiological processes by relating changes in the extracellular environment to intracellular functions via activation of heterotrimeric G-proteins. However, G-protein activity is also modulated by a family of proteins called regulators of G-protein signalling (RGS), which are classified into six subfamilies. RGS10 belongs to the subgroup D/R12 and is known to act specifically on activated forms of three Gα proteins (Gαi3, Gαz and Gαo but not Gαs). It is abundantly expressed in brain and immune tissues and has been implicated in the pathophysiology of schizophrenia. The RGS domain of RGS10 was cloned, purified, complexed with human Gαi3 and crystallized. The crystals containing both RGS and Gαi3 belong to space group P43212 (or P41212), with unit-cell parameters a = 99.88, b = 99.88, c = 144.59 Å, α = β = γ = 90°. A full set of diffraction data were collected to 2.5 Å resolution at 100 K using synchrotron radiation at Pohang beamline 4A.

Original languageEnglish
Pages (from-to)831-833
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number9
Publication statusPublished - 2005 Sept

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


Dive into the research topics of 'Crystallization and preliminary X-ray crystallographic analysis of human RGS10 complexed with Gαi3'. Together they form a unique fingerprint.

Cite this