Related Experiment Video
Updated: Aug 23, 2026

Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Crystallization and preliminary X-ray analysis of brazzein, a new sweet protein
K Ishikawa1, K Ishikawa, M Ota
1Central Research Laboratories, Ajinomoto Co., Inc., Kawasaki, Japan.
Abstract:
Brazzein is a sweet protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble protein sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
More Related Videos
Related Concept Videos
Recrystallization: Solid–Solution Equilibria
X-ray Diffraction of Biological Samples
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are scattered by the electron clouds around the sample atoms. The X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
Crystal Growth: Principles of Crystallization
Initiating crystallization involves manipulating the concentration of the solute and the temperature of the solution. Since crystal growth occurs when the ratio of concentration and solubility of the solute in the solvent – the...

