Monterroso, BegoñaAhijado Guzmán, RubénReija, BelénAlfonso, CarlosZorrilla, SilviaMinton, AllenRivas, Germán2024-01-092024-01-092012Begoña Monterroso, Rubén Ahijado-Guzmán, Belén Reija, Carlos Alfonso, Silvia Zorrilla, Allen P. Minton, and Germán Rivas Biochemistry 2012 51 (22), 4541-4550 DOI: 10.1021/bi300401b0006-296010.1021/bi300401bhttps://hdl.handle.net/20.500.14352/92115The assembly of the bacterial cell division FtsZ protein in the presence of constantly replenished GTP was studied as a function of Mg2+ concentration (at neutral pH and 0.5 M potassium) under steady-state conditions by sedimentation velocity, concentration-gradient light scattering, fluorescence correlation spectroscopy, and dynamic light scattering. Sedimentation velocity measurements confirmed previous results indicating cooperative appearance of a narrow size distribution of finite oligomers with increasing protein concentration. The concentration dependence of light scattering and diffusion coefficients independently verified the cooperative appearance of a narrow distribution of high molecular weight oligomers, and in addition provided a measurement of the average size of these species, which corresponds to 100 ± 20 FtsZ protomers at millimolar Mg2+ concentration.engjournal articlehttps://doi.org/10.1021/bi300401brestricted access544Ciencias BiomédicasQuímica física (Química)2307 Química Física