Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1.
RuvBL1, an evolutionary highly conserved protein related to the AAA+ family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 A and three molecules in the asymmetric unit.
Gorynia
Sabine
S
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras, Portugal.
Matias
Pedro M
PM
Gonçalves
Susana
S
Coelho
Ricardo
R
Lopes
Gonçalo
G
Thomaz
Mónica
M
Huber
Martina
M
Haendler
Bernard
B
Donner
Peter
P
Carrondo
Maria Arménia
MA
D000074183:ATPases Associated with Diverse Cellular Activities; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011994:Recombinant Proteins; C061260:RuvB protein, Bacteria; D000074183:ATPases Associated with Diverse Cellular Activities; D004265:DNA Helicases; C486549:RUVBL1 protein, human