J Mol Biol. 1992 Jul 20;226(2):555-7.

Purification and crystallization of human cathepsin D.

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European Molecular Biology Laboratory, Heidelberg, Germany.

Abstract

The two-chain form of human cathepsin D was purified from human spleen with a method utilizing an ion exchange chromatography step prior to the pepstatin affinity column normally used to purify aspartic proteases. The protein was crystallized from 21% polyethylene glycol 8000 at pH 4.0 using the hanging drop vapour diffusion method. Small crystals were used as seeds to grow crystals suitable for X-ray data collection. The crystals diffract to a resolution of 3.2 A and have space group P2(1)2(1)2(1) with unit cell dimensions a = 59.9 A, b = 99.6 A, c = 133.6 A. There are two molecules in the asymmetric unit.

PMID:: 1640466; [PubMed - indexed for MEDLINE]

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Cathepsin D

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