Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution
✍ Scribed by G.N. Murshudov; W.R. Melik-Adamyan; A.I. Grebenko; V.V. Barynin; A.A. Vagin; B.K. Vainshtein; Z. Dauter; K.S. Wilson
- Book ID
- 115926596
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 593 KB
- Volume
- 312
- Category
- Article
- ISSN
- 0014-5793
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The three-dimensional structure of the multisubunit allosteric enzyme, aspartate transcarbamylase, has been determined t o 5.5 a resolution. An unusual feature of the molecule is a large central aqueous cavity 50 a X 50 a X 25 a, into which the active sites face. Access t o the central cavity and th
## Abstract The protein actinoxanthin (isolated from __Actinomyces globisporus__—molecular weight, 10,300; 107 amino acid residues) crystallizes in space group __P__2~1~2~1~2~1~ with cell dimensions: __a__ = 30.9 Å, __b__ = 48.8 Å, __c__ = 64.1 Å, and __Z__ = 4. The three‐dimensional structure of a