Km. Stephens et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF I-CREI - A GROUP-I INTRON-ENCODED ENDONUCLEASE FROM CHLAMYDOMONAS-REINHARDTII, Proteins, 28(1), 1997, pp. 137-139
Group I intron endonuclease I-CreI is encoded by an open reading frame
contained within a self-splicing intron in the Chlamydomonas reinhard
tii chloroplast 235 rRNA gene, I-CreI initiates the lateral transfer o
r homing of this intron by specifically recognizing and cleaving a pse
udopalindromic 19-24 bp homing site in chloroplast 235 rRNA genes that
lack the intron. The gene encoding this enzyme has been subcloned, an
d the protein product has been purified and crystallized. The crystals
belong to space group P321, with unit cell dimensions a = b = 78.2 An
gstrom c = 67.4 Angstrom. 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 Angstrom(3)/Da. The crystals diffract to at l
east 3.0 Angstrom resolution after flash-cooling, when using a rotatin
g anode x-ray source and an RAXIS image plate detector. (C) 1997 Wiley
-Liss, Inc.