Production of crystallizable human chymase from a Bacillus subtilis system.

Abstract:

:A Bacillus subtilis strain deficient in seven extracellular proteases was used to produce human mast cell chymase and is a viable expression system for serine proteases and other classes of proteins. Chymase is produced at 0.3-0.5 mg/l and is purified by three chromatography steps. Two crystal forms of PMSF-treated chymase were optimized. The first is C2 with a=47.94 A, b=85.23 A, c=174.18 A, beta=96.74 degrees, and diffracts to at least 2.1 A, while the second is P212121, with cell dimensions a=43.93 A, b=58.16 A, and c=86.09 A, and a diffraction limit of approximately 1.9 A. The first crystal form has either three or four molecules/asymmetric unit, while the second has one molecule/asymmetric unit.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

McGrath ME,Osawa AE,Barnes MG,Clark JM,Mortara KD,Schmidt BF

doi

10.1016/s0014-5793(97)00962-9

subject

Has Abstract

pub_date

1997-08-25 00:00:00

pages

486-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00962-9

journal_volume

413

pub_type

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