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Crystallization and initial crystallographic results for pepstatin A inhibited bovine cathepsin D.

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 A and have space group P2(1)2(1)2(1) with unit cell dimensions a = 74.8 A, b = 76.0 A, c = 157.7 A. 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 A and 3.2 degrees, respectively, and a crystallographic R factor of 17%.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Bieber F,Brachvogel V,Arni R,Fusek M,Metcalf P

doi

10.1016/0022-2836(92)90539-v

keywords:

subject

Has Abstract

pub_date

1992-10-20 00:00:00

pages

1265-8

issue

4

eissn

0022-2836

issn

1089-8638

pii

0022-2836(92)90539-V

journal_volume

227

pub_type

杂志文章

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