Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 01; 68(Pt 2):244-6.AC
Abstract
Orotate phosphoribosyltransferase (OPRT) catalyzes the Mg(2+)-dependent condensation of orotic acid (OA) with 5-α-D-phosphorylribose 1-diphosphate (PRPP) to yield diphosphate (PP(i)) and the nucleotide orotidine 5'-monophosphate. OPRT from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg(2+). The crystal exhibited tetragonal symmetry, belonging to space group P4(1) or P4(3), with unit-cell parameters a = b = 49.15, c = 226.94 Å. X-ray diffraction data were collected to 2.5 Å resolution at 100 K using a synchrotron-radiation source.
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Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
22298010
Citation
Takashima, Yasuhide, et al. "Crystallization and Preliminary X-ray Diffraction Analysis of Orotate Phosphoribosyltransferase From the Human Malaria Parasite Plasmodium Falciparum." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 68, no. Pt 2, 2012, pp. 244-6.
Takashima Y, Mizohata E, Tokuoka K, et al. Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68(Pt 2):244-6.
Takashima, Y., Mizohata, E., Tokuoka, K., Krungkrai, S. R., Kusakari, Y., Konishi, S., Satoh, A., Matsumura, H., Krungkrai, J., Horii, T., & Inoue, T. (2012). Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 68(Pt 2), 244-6. https://doi.org/10.1107/S1744309111043247
Takashima Y, et al. Crystallization and Preliminary X-ray Diffraction Analysis of Orotate Phosphoribosyltransferase From the Human Malaria Parasite Plasmodium Falciparum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):244-6. PubMed PMID: 22298010.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum.
AU - Takashima,Yasuhide,
AU - Mizohata,Eiichi,
AU - Tokuoka,Keiji,
AU - Krungkrai,Sudaratana R,
AU - Kusakari,Yukiko,
AU - Konishi,Saki,
AU - Satoh,Atsuko,
AU - Matsumura,Hiroyoshi,
AU - Krungkrai,Jerapan,
AU - Horii,Toshihiro,
AU - Inoue,Tsuyoshi,
Y1 - 2012/01/27/
PY - 2011/09/12/received
PY - 2011/10/19/accepted
PY - 2012/2/3/entrez
PY - 2012/2/3/pubmed
PY - 2012/4/12/medline
SP - 244
EP - 6
JF - Acta crystallographica. Section F, Structural biology and crystallization communications
JO - Acta Crystallogr Sect F Struct Biol Cryst Commun
VL - 68
IS - Pt 2
N2 - Orotate phosphoribosyltransferase (OPRT) catalyzes the Mg(2+)-dependent condensation of orotic acid (OA) with 5-α-D-phosphorylribose 1-diphosphate (PRPP) to yield diphosphate (PP(i)) and the nucleotide orotidine 5'-monophosphate. OPRT from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg(2+). The crystal exhibited tetragonal symmetry, belonging to space group P4(1) or P4(3), with unit-cell parameters a = b = 49.15, c = 226.94 Å. X-ray diffraction data were collected to 2.5 Å resolution at 100 K using a synchrotron-radiation source.
SN - 1744-3091
UR - https://www.unboundmedicine.com/medline/citation/22298010/Crystallization_and_preliminary_X_ray_diffraction_analysis_of_orotate_phosphoribosyltransferase_from_the_human_malaria_parasite_Plasmodium_falciparum_
L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309111043247
DB - PRIME
DP - Unbound Medicine
ER -