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

ABSTRACT: 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%.

SUBMITTER: Takeshita D

PROVIDER: S-EPMC2242961 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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

Takeshita Daijiro D Zenno Shuhei S Lee Woo Cheol WC Saigo Kaoru K Tanokura Masaru M

Acta crystallographica. Section F, Structural biology and crystallization communications 20060610 Pt 7

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. ...[more]

PMID: 16820686

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