| Literature DB >> 1901570 |
M B Sherman1, E V Orlova, E A Smirnova, S Hovmöller, N A Zorin.
Abstract
The three-dimensional structure of the nickel-containing hydrogenase from Thiocapsa roseopersicina has been determined at a resolution of 2 nm in the plane and 4 nm in the vertical direction by electron microscopy and computerized image processing on microcrystals of the enzyme. The enzyme forms a large ring-shaped complex containing six each of the large (62-kDa) and small (26-kDa) subunits. The complex is very open, with six well-separated dumbbell-shaped masses surrounding a large cylindrical hole. Each dumbbell is interpreted as consisting of one large and one small subunit.Entities:
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Year: 1991 PMID: 1901570 PMCID: PMC207823 DOI: 10.1128/jb.173.8.2576-2580.1991
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490