Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II

Citation
Rj. Guan et al., Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II, ACT CRYST D, 56, 2000, pp. 918-919
Citations number
24
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
7
Pages
918 - 919
Database
ISI
SICI code
0907-4449(200007)56:<918:CAPXAO>2.0.ZU;2-V
Abstract
Mabinlin II is a sweet protein with the highest known thermostablility and is isolated from the seeds of Capparis masaikai Lev1. grown in south China. Two crystal forms of mabinlin II were obtained using the hanging-drop vapo ur-diffusion method. One of them diffracts to 2.8 Angstrom resolution and b elongs to space group P2, with unit-cell parameters a = 50.16, b = 50.17, c = 76.60 Angstrom, beta = 99.6 degrees. There are four molecules per asymme tric unit, with a solvent content of 35.3%.