Purification and crystallization of human cathepsin D.
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.
Fusek
M
M
European Molecular Biology Laboratory, Heidelberg, Germany.
Baudys
M
M
Metcalf
P
P
D002402:Cathepsin D / Q000302:isolation & purification* / Q000648:ultrastructure; D003461:Crystallography; D006801:Humans; D008970:Molecular Weight; D011487:Protein Conformation; D014961:X-Ray Diffraction
D002402:Cathepsin D