Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|62|7|656-658
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.62, Iss.7, 2006-07, pp. : 656-658
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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 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%.
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