Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNA(Gly) acceptor-stem microhelix.
The tRNA(Gly) and glycyl-tRNA synthetase (GlyRS) system is an evolutionary special case within the class II aminoacyl-tRNA synthetases because two divergent types of GlyRS exist: an archaebacterial/human type and an eubacterial type. The tRNA identity elements which determine the correct aminoacylation process are located in the aminoacyl domain of tRNA(Gly). To obtain further insight concerning structural investigation of the identity elements, the Escherichia coli seven-base-pair tRNA(Gly) acceptor-stem helix was crystallized. Data were collected to 2.0 A resolution using synchrotron radiation. Crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 35.35, c = 130.82 A, alpha = beta = 90, gamma = 120 degrees and two molecules in the asymmetric unit.
Förster
Charlotte
C
Institute of Chemistry and Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany.
Perbandt
Markus
M
Brauer
Arnd B E
AB
Brode
Svenja
S
Fürste
Jens P
JP
Betzel
Christian
C
Erdmann
Volker A
VA
D003460:Crystallization; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D011487:Protein Conformation; D012353:RNA, Transfer, Gly / Q000032:analysis* / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods*
D029968:Escherichia coli Proteins; D012353:RNA, Transfer, Gly