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- Publisher
- Wiley
- Copyright
- Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309107045393
- pmid
- 18007042
- Publisher site
- See Article on Publisher Site
Abstract
SPCI, a Kunitz‐type chymotrypsin inhibitor, is a 180‐amino‐acid polypeptide isolated from Schizolobium parahyba seeds. This inhibitor has been characterized as a highly stable protein over a broad pH and temperature range. SPCI was crystallized using a solution containing 0.1 M sodium acetate trihydrate buffer pH 4.6, 33%(v/v) PEG 2000 and 0.2 M ammonium sulfate. Data were collected to 1.80 Å resolution from a single crystal of SPCI under cryogenic conditions. The protein crystallized in space group P21212, with unit‐cell parameters a = 40.01, b = 71.58, c = 108.68 Å and an Rmerge of 0.052. The structure of SPCI has been solved by molecular replacement using the known structure of the Kunitz‐type trypsin inhibitor from Delonix regia (PDB code 1r8n) as the search model.
Journal
Acta Crystallographica Section F – Wiley
Published: Nov 1, 2007