EC Number   |
|---|
   3.6.4.B7 | - |
| 3.6.4.B7 | crystal structure analysis, enzyme with bound AMP-PNP, PDB ID 1T4G |
| 3.6.4.B7 | crystal structure analysis, PDB ID 1PZN |
| 3.6.4.B7 | crystal structure analysis, PDB ID 1T4G |
| 3.6.4.B7 | crystal structure analysis, PDB IDs 2DFL and 2BKE |
| 3.6.4.B7 | crystal structure of full-length enzyme, quality crystals are grown at 4°C using the hanging drop vapour diffusion method against a reservoir containing 0.5 ml 0.1 M TrisHCl, pH 9.5 with 10% (v/v) tert-butanol, resolution of 3.2 A. crystal structure reveals a conformation of fine filaments in the absence of nucleotides |
| 3.6.4.B7 | crystallization of a hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain, crystals are grown by the hanging drop method The RadA hexamers further assemble into two-ringed assemblies |
| 3.6.4.B7 | crystallized using the hanging drop vapor diffusion method, crystal structure of Sulfolobus solfataricus RadA overwound right-handed filament with three monomers per helical pitch. This structure reveals conformational details of the first ssDNA binding disordered loop (denoted L1 motif) and the dsDNA binding N-terminal domain (NTD). L1 and NTD together form an outwardly open palm structure on the outer surface of the helical filament. Inside this palm structure, five conserved basic amino acid residues (K27, K60, R117, R223 and R229) surround a 25 A pocket that is wide enough to accommodate anionic ssDNA, dsDNA or both. These five positively charged residues are essential for DNA binding and for RadA-catalyzed D-loop formation |
| 3.6.4.B7 | expression as a MBP-RadA-His6-fusion protein in Escherichia coli |
| 3.6.4.B7 | hanging drop crystallization method at 21 °C. Enzyme in complex with AMP-PNP and K+ (2.7 A resolution), enzyme in complex with AMP-PNP (2.9 A resolution), enzyme in complex with ADP (2.4 A resolution) |
