Crystallization and preliminary X-ray studies of I-CreI: a group I intron-encoded endonuclease from C. reinhardtii

Autor:	K M, Stephens, R J, Monnat, P J, Heath, B L, Stoddard
Rok vydání:	1997
Předmět:	Chloroplasts Escherichia coli Animals Fractional Precipitation RNA Catalytic DNA Restriction Enzymes Crystallization Crystallography X-Ray Chlamydomonas reinhardtii Introns
Zdroj:	Proteins. 28(1)
ISSN:	0887-3585
Popis:	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 = b = 78.2 A, c = 67.4 A. 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 A3/Da. The crystals diffract to at least 3.0 A resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::2de57535e760deac3e02b83a2abb2ace https://pubmed.ncbi.nlm.nih.gov/9144800 Zobrazit plný text záznamu Plný text