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Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2006 Jan 01; Vol. 62 (Pt 1), pp. 61-6. Date of Electronic Publication: 2005 Dec 16. - Publication Year :
- 2006
-
Abstract
- 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.
- Subjects :
- ATPases Associated with Diverse Cellular Activities
Amino Acid Sequence
Bacterial Proteins chemistry
Carrier Proteins isolation & purification
Conserved Sequence
Crystallization
Crystallography, X-Ray
DNA Helicases isolation & purification
Evolution, Molecular
Humans
Molecular Sequence Data
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins isolation & purification
Sequence Homology, Amino Acid
Carrier Proteins chemistry
Carrier Proteins genetics
DNA Helicases chemistry
DNA Helicases genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 62
- Issue :
- Pt 1
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 16511264
- Full Text :
- https://doi.org/10.1107/S1744309105041400