Crystallization and preliminary X-ray analysis of the PIN domain of human EST1A

Journal Article · Sat Jul 01 04:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106020057· OSTI ID:22360209

Takeshita, Daijiro ^[1]; Zenno, Shuhei ^[2]; Lee, Woo Cheol ^[1]; Saigo, Kaoru ^[2]; Tanokura, Masaru ^[1]

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1. 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)
2. Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033 (Japan)

The PIN domain of human EST1A was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. 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 Å, β = 119.3°, and diffracted X-rays to 1.8 Å resolution. The asymmetric unit contained two molecules of the PIN domain and the solvent content was 57%.

• OSTI ID: 22360209
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ELONGATION
MOLECULES
RESOLUTION
SOLVENTS
SPACE GROUPS