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- W2092269144 abstract "Cathepsin D was purified from bovine liver by a method using two pepstatin A affinity columns. The eluted protein was combined with pepstatin A and the complex crystallized from 15% polyethylene glycol 8000 at pH 5·9. The crystals diffract to a resolution of 3·0 Å and have space group P212121 with unit cell dimensions a = 74·8 Å, b = 76·0 Å, c = 157·7 Å. There are two molecules in the asymmetric unit. The structure was solved by molecular replacement using a pepsin search model and both molecules showed clearly interpretable density in the position expected for pepstatin A in a preliminary difference map. The refined model has r.m.s. deviations from ideal bond lengths and angles of 0·014 Å and 3·2 °, respectively, and a crystallographic `R factor of 17%." @default.
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- W2092269144 date "1992-10-01" @default.
- W2092269144 modified "2023-10-16" @default.
- W2092269144 title "Crystallization and initial crystallographic results for pepstatin A inhibited bovine cathepsin D" @default.
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- W2092269144 doi "https://doi.org/10.1016/0022-2836(92)90539-v" @default.
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