Applications of thermal-gradients method for the optimization of α-amylase crystallization conditions based on dynamic and static light scattering data

Autor:	L.F. Delboni, J. Iulek, A.C.R. da Silva, Abel Moreno, R. Burger
Rok vydání:	2002
Předmět:	Diffraction Chemistry Organic Chemistry Resolution (electron density) Analytical chemistry Crystal growth Analytical Chemistry Characterization (materials science) law.invention Inorganic Chemistry law Thermal Static light scattering Crystallization Protein crystallization Spectroscopy
Zdroj:	Journal of Molecular Structure. 604:253-260
ISSN:	0022-2860
DOI:	10.1016/s0022-2860(01)00663-9
Popis:	The expression, purification, crystallization, and characterization by X-ray diffraction of α-amylase are described here. Dynamic and static light scattering methods with a temperature controller was used to optimize the crystallization conditions of α-amylase from Bacillus stearothermophilus an important enzyme in many fields of industrial activity. After applying thermal gradients for growing crystals, X-ray cryo-crystallographic methods were employed for the data collection. Crystals grown by these thermal-gradients diffracted up to a maximum resolution of 3.8 A, which allowed the determination of the unit cell constants as follows: a=61.7 A , b=86.7 A , c=92.2 A and space group C222 (or C2221).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::6871b14a0703c7ed4950e04934599113 https://doi.org/10.1016/s0022-2860(01)00663-9 Zobrazit plný text záznamu Full Text from ScienceDirect