## Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a 5 47.24 ร , b 5 63.59 ร , and c 5 62.57 ร . They belong to spac
Crystallization and X-ray diffraction studies of glutathione S-transferase from Escherichia coli
โ Scribed by Motohiko Nishida; Shigeharu Harada; Yoshinori Satow; Hideshi Inoue; Kenji Takahashi
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 323 KB
- Volume
- 168
- Category
- Article
- ISSN
- 0022-0248
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals
## Abstract The Cu, Zn superoxide dismutase (Cu, Zn SOD) originally isolated from the periplasmic space of __Escherichia coli__ has been cloned and overexpressed in the __E. coli__ strain BMH 71/18. The protein has been purified as a single component of 17,000 Da, corresponding to one subunit of th
Human procathepsin L has been expressed in the yeast Pichiapastoris and its inactive (Cys25Ser) and unglycosylated (ThrllOAla) mutant purified, concentrated to 4 mglml, and crystallized by vapor diffusion against solution containing 1.4 M (Na,K)PO, buffer, pH 7.8. Crystal size was increased by multi
## Abstract Nonglycosylated ฮฑโamylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2โmethylโ2,4โpentanediol as the precipitant in the presence of CaCl~2~ at pH 9.0. The crystals are orthorhombic, space group __P__2~1~2~1~2~1~ with unit cel
## Abstract 5โAminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5โaminolaevulinic acid. Both __Escherichia coli__ and __Saccharomyces cerevisiae__ ALADs are homoโoctameric enzymes which depend on Zn^2+^ for catalytic activity and are potently i