Abstract
Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.
| Original language | English |
|---|---|
| Pages (from-to) | 332-335 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 69 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2013 Mar 1 |
| Externally published | Yes |
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Keywords
- peptidyl-tRNA hydrolase
- Thermus thermophilus
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics
- Condensed Matter Physics
Cite this
Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8. / Matsumoto, Ami; Shimizu, Yoshihiro; Takemoto, Chie; Ueda, Takuya; Uchiumi, Toshio; Ito, Kosuke.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 3, 01.03.2013, p. 332-335.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8
AU - Matsumoto, Ami
AU - Shimizu, Yoshihiro
AU - Takemoto, Chie
AU - Ueda, Takuya
AU - Uchiumi, Toshio
AU - Ito, Kosuke
PY - 2013/3/1
Y1 - 2013/3/1
N2 - Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.
AB - Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.
KW - peptidyl-tRNA hydrolase
KW - Thermus thermophilus
UR - http://www.scopus.com/inward/record.url?scp=84875518231&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84875518231&partnerID=8YFLogxK
U2 - 10.1107/S1744309113003424
DO - 10.1107/S1744309113003424
M3 - Article
C2 - 23519816
AN - SCOPUS:84875518231
VL - 69
SP - 332
EP - 335
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 3
ER -