The protein C pathway plays an important role in the control and regulation of the blood coagulation cascade and prevents the propagation of the clotting process on the endothelium surface. In physiological systems, protein C activation is catalyzed by thrombin, which requires thrombomodulin as a co
Crystallization and preliminary x-ray studies of I-CreI: a group I intron-encoded endonuclease from C. reinhardtii
โ Scribed by Kathryn M. Stephens; Raymond J. Monnat Jr.; Patrick J. Heath; Barry L. Stoddard
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 78 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
โฆ Synopsis
Group I intron endonuclease I-CreI is encoded by an open reading frame contained within a self-splicing intron in the Chlamydomonas reinhardtii chloroplast 23S rRNA gene. I-CreI initiates the lateral transfer or homing of this intron by specifically recognizing and cleaving a pseudopalindromic 19-24 bp homing site in chloroplast 23S rRNA genes that lack the intron. The gene encoding this enzyme has been subcloned, and the protein product has been purified and crystallized. The crystals belong to space group P321, with unit cell dimensions a 5 b 5 78.2 ร , c 5 67.4 ร . The crystal unit cell is consistent with an asymmetric unit consisting of the enzyme monomer. The specific volume of this unit cell is 3.3 ร 3 /Da. The crystals diffract to at least 3.0 ร resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector.
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
Conformational energy computations on a derivative and a homo-dipeptide of C"\*"-diethylglycine were performed. In both cases the Nand C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the C"3"-diethylglycine residues are conformationally restricted
Interaction of Trimethylsilyl and Trimethylstannyl Substituents with C-O Bonds at the ฮณ Position. Results from X-Ray Structural Studies and Solvolysis Studies of (I)-(IV). --(GREEN, A.