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 Lettjournal_title
FEBS lettersauthors
McGrath ME,Osawa AE,Barnes MG,Clark JM,Mortara KD,Schmidt BFdoi
10.1016/s0014-5793(97)00962-9subject
Has Abstractpub_date
1997-08-25 00:00:00pages
486-8issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00962-9journal_volume
413pub_type
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