Purification and Crystallographic Analysis of a Novel Cold-Active Esterase (HaEst1) from Halocynthiibacter arcticus
- Authors
- Jeon, Sangeun; Hwang, Jisub; Yoo, Wanki; Chang, Joo Won; Do, Hackwon; Kim, Han-Woo; Kim, Kyeong Kyu; Lee, Jun Hyuck; Kim, T. Doohun
- Issue Date
- Feb-2021
- Publisher
- MDPI
- Keywords
- esterase; enzyme assay; crystallization; diffraction
- Citation
- CRYSTALS, v.11, no.2, pp 1 - 7
- Pages
- 7
- Journal Title
- CRYSTALS
- Volume
- 11
- Number
- 2
- Start Page
- 1
- End Page
- 7
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159380
- DOI
- 10.3390/cryst11020170
- ISSN
- 2073-4352
- Abstract
- This report deals with the purification, characterization, and a preliminary crystallographic study of a novel cold-active esterase (HaEst1) from Halocynthiibacter arcticus. Primary sequence analysis reveals that HaEst1 has a catalytic serine in G-x-S-x-G motif. The recombinant HaEst1 was cloned, expressed, and purified. SDS-PAGE and zymographic analysis were carried out to characterize the properties of HaEst1. A single crystal of HaEst1 was obtained in a solution containing 10% (w/v) PEG 8000/8% ethylene glycol, 0.1 M Hepes-NaOH, pH 7.5. Diffraction data were collected to 2.10 angstrom resolution with P2(1) space group. The final R-merge and R-p.i.m values were 7.6% and 3.5% for 50-2.10 angstrom resolution. The unit cell parameters were a = 35.69 angstrom, b = 91.21 angstrom, c = 79.15 angstrom, and beta = 96.9 degrees.
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