Crystallization of Clonorchis sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengthsopen access
- Authors
- Han, YH; Chung, YH; Kim, TY; Hong, SJ; Choi, JD; Chung, YJ
- Issue Date
- Apr-2001
- Publisher
- MUNKSGAARD INT PUBL LTD
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.57, pp 579 - 581
- Pages
- 3
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Volume
- 57
- Start Page
- 579
- End Page
- 581
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25234
- DOI
- 10.1107/S0907444900019314
- ISSN
- 0907-4449
- Abstract
- A Clonorchis sinensis 26 kDa glutathione S-transferase (CsGST) and its fusion proteins containing 14 and 48 amino-acid peptides at the N-terminus have been crystallized using polyethylene glycol monomethylether 550 as a precipitant. Crystals of the three proteins show very similar crystal properties: they diffract to at least 2.3 Angstrom resolution and belong to the orthorhombic space group P2(1)2(1)2(1). The unit-cell parameters of CsGST crystals were a = 66.64 (1), b = 68.91 (1), c = 123.41 (2) Angstrom, which are very close to those of the crystals of the two fusion proteins. In addition, CsGST fusion proteins containing varying extents of N-terminal-extended peptides are incorporated into a crystal, indicating that the extended peptides have little effect on crystal packing. These results suggest that the crystallization system of CsGST/peptide fusion protein may be generally applicable to obtain crystals of small peptides.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Medicine > College of Medicine > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25234)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.