Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV fromThermotoga maritima
Year: 2009
Type: article
Abstract: The DNA-repair enzyme endonuclease IV from the thermophilic bacterium Thermotoga maritima MSB8 (reference sequence NC_000853) has been expressed in Escherichia coli and crystallized for X-ray analysis. T. maritima endonuclease IV is a 287-amino-acid protein with 32% sequence identity to E. coli endonuclease IV. The protein was purified to homogeneity and was crystallized using the sitting-drop vapor-diffusion method. The protein crystallized in space group P6(1), with one biological molecule in the asymmetric unit, corresponding to a Matthews coefficient of 2.39 A(3) Da(-1) and 47% solvent content. The unit-cell parameters of the crystals were a = b = 123.2, c = 35.6 A. Microseeding and further optimization yielded crystals with an X-ray diffraction limit of 2.36 A. A single 70 degrees data set was collected and processed, resulting in an overall R(merge) and a completeness of 9.5% and 99.3%, respectively.
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
Awards: G1019100964, G1026679911, G121915436, G1528409558, G1645119126, G166562317, G1678787968, G1756342139, G18202666, G203625172, G2123841078, G2988778103, G3049477530, G3121793570, G313676650, G4423657506, G450780475, G5726405315, G572720644, G574648691, G6486853205, G675320460, G6911681599, G7769062580, G807938293, G8269158468, G8906985441, G8943143067
OpenAlex ID: W1972205302