𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Crystallization and analysis of the subunit assembly and quaternary structure of imidazoleglycerol phosphate dehydratase from Saccharomyces cerevisiae

✍ Scribed by Wilkinson, K. W. ;Baker, P. J. ;Rice, D. W. ;Rodgers, H. F. ;Stillman, T. J. ;Hawkes, T. ;Thomas, P. ;Edwards, L.

Book ID
114529177
Publisher
International Union of Crystallography
Year
1995
Tongue
English
Weight
296 KB
Volume
51
Category
Article
ISSN
0907-4449

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Crystallization and preliminary structur
Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae
✍ Serge Berthet; Jeronimo Bravo; Maria J. Mate; Ignacio Fita; Leena M. Nykyri; Fra πŸ“‚ Article πŸ“… 2008 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 349 KB

Yeast peroxisomal catalase A, obtained at high yields by over expression of the C-terminally modified gene from a 2 mu-plasmid, has been crystallized in a form suitable for high resolution X-ray diffraction studies. Brownish crystals with bipyrimidal morphology and reaching ca. 0.8 mm in size were p

Crystallization of 5-aminolaevulinic aci
Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals
✍ P.T. Erskine; J. Cooper; R. Lambert; G. Lewis; S.P. Wood; P.M. Shoolingin-Jordan πŸ“‚ Article πŸ“… 1997 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 330 KB

## Abstract 5‐Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5‐aminolaevulinic acid. Both __Escherichia coli__ and __Saccharomyces cerevisiae__ ALADs are homo‐octameric enzymes which depend on Zn^2+^ for catalytic activity and are potently i