Crystallization and preliminary studies of lima bean trypsin inhibitor
β Scribed by Cleopas Samudzi; Steven Schroeder; Scott Griffith; Xin Chen; Thomas P. Quinn
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 74 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0887-3585
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β¦ Synopsis
Crystals of lima bean trypsin inhibitor (LBTI) were obtained by using the vapor phase equilibration technique with sodium/potassium tartrate as the precipitating agent. The space group was determined to be cubic, I2 1 3 with a 5 110.2 Γ . These crystals diffract to about 1.9 Γ resolution. Preliminary analysis of self-rotation maps (calculated from native x-ray intensity data) suggests the presence of two monomers in the asymmetric unit. LBTI is very thermostable and retains activity even after boiling for 10 minutes. This property is exploited as part of its purification procedure.
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## Abstract Neurotrophinβ3 (NTβ3) has been crystallized in 2 forms. Orthorhombic crystals, space group P2~1~2~1~2, diffracted to 2.8 Γ and have cell dimensions __a__ = 39.1 Γ , __b__ = 54.0 Γ , and __c__ = 65.5 Γ . The second form is space group P4~3~2~1~2, with cell dimensions __a__ = __b__ = 67.1 Γ ,
## Abstract The protein, trypsin inhibitor and lipid of the seeds from 15 New Guinea and 15 Thai winged bean varieties grown in Malaysia were analysed. The results show that winged bean seeds have a high protein content, ranging from 27.8 to 47.2% (based on dry seed wt). The trypsin inhibitor conte