Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 62, Issue -, Pages 656-658Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309106020057
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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 angstrom, beta = 119.3 degrees, and diffracted X-rays to 1.8 angstrom resolution. The asymmetric unit contained two molecules of the PIN domain and the solvent content was 57%.
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