Crystallization and preliminary X-ray analysis of the PIN domain of human EST1A.
Human EST1A (ever shorter telomeres 1A) is associated with most or all active telomerase in cell extracts and is involved either directly or indirectly in telomere elongation and telomere capping. The C-terminal region of EST1A contains the PIN (PilT N-terminus) domain, a putative nuclease domain. The PIN domain of human EST1A was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group C2, with unit-cell parameters a = 107.3, b = 51.6, c = 100.5 angstroms, beta = 119.3 degrees, and diffracted X-rays to 1.8 angstroms resolution. The asymmetric unit contained two molecules of the PIN domain and the solvent content was 57%.
Takeshita
Daijiro
D
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Zenno
Shuhei
S
Lee
Woo Cheol
WC
Saigo
Kaoru
K
Tanokura
Masaru
M
D003460:Crystallization; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D019098:Telomerase / Q000737:chemistry* / Q000302:isolation & purification; D016615:Telomere / Q000378:metabolism; D014961:X-Ray Diffraction; D004722:Endoribonucleases
D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D019098:Telomerase; C512261:SMG6 protein, human; D004722:Endoribonucleases