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.
MeSH terms
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ATPases Associated with Diverse Cellular Activities
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics*
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Carrier Proteins / isolation & purification
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Conserved Sequence
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Crystallization
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Crystallography, X-Ray
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DNA Helicases / chemistry*
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DNA Helicases / genetics*
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DNA Helicases / isolation & purification
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Evolution, Molecular
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Humans
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Molecular Sequence Data
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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Carrier Proteins
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Recombinant Proteins
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RuvB protein, Bacteria
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ATPases Associated with Diverse Cellular Activities
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DNA Helicases
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RUVBL1 protein, human