2004
DOI: 10.1107/s0907444904001544
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Characterization, crystallization and preliminary X-ray analysis of bifunctional dihydrofolate reductase–thymidylate synthase fromPlasmodium falciparum

Abstract: In the paper by Chitnumsub et al. (2004) the details for one of the authors were given incorrectly. The name of the second author is Jirundon Yuvaniyama (instead of Yavaniyama) and his af®liation is Center for Protein Structure and Function and Department of Biochemistry, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand. The full-length pfdhfr-ts genes of the wild-type TM4/8.2 and the double mutant K1CB1 (C59R+S108N) from the genomic DNA of the corresponding Plasmodium falciparum … Show more

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Cited by 53 publications
(54 citation statements)
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“…Plasmids pET17b (Novagen), pETpfTM4 (harboring the WT pfdhfr-ts gene [4]), and pETpfK1 (harboring the C59R S108N mutation [4]) were individually transformed into BL21(DE3) bacteria, while pETpvDHFR-TS and pETpvSP21 were individually transformed into BL21(DE3)pLysS bacteria. BL21(DE3) carrying plasmid was grown on LB agar supplemented with 100 g ml Ϫ1 ampicillin, whereas BL21(DE3)pLysS-transformed cells were grown on LB agar supplemented with 100 g ml Ϫ1 ampicillin and 34 g ml Ϫ1 chloramphenicol.…”
mentioning
confidence: 99%
“…Plasmids pET17b (Novagen), pETpfTM4 (harboring the WT pfdhfr-ts gene [4]), and pETpfK1 (harboring the C59R S108N mutation [4]) were individually transformed into BL21(DE3) bacteria, while pETpvDHFR-TS and pETpvSP21 were individually transformed into BL21(DE3)pLysS bacteria. BL21(DE3) carrying plasmid was grown on LB agar supplemented with 100 g ml Ϫ1 ampicillin, whereas BL21(DE3)pLysS-transformed cells were grown on LB agar supplemented with 100 g ml Ϫ1 ampicillin and 34 g ml Ϫ1 chloramphenicol.…”
mentioning
confidence: 99%
“…The relative PfDHFR activity of each mutant compared to wild-type enzyme was determined from crude protein extracts. Those with relative crude activity higher than 3% were further purified by methotrexate-Sepharose affinity chromatography (17) and anion exchange as previously described (2,9).…”
Section: Methodsmentioning
confidence: 99%
“…The bifunctional DHFR-TS enzymes of both wild-type strain TM4 and the A16VϩS108T mutant strain T9/94 of P. falciparum were cloned, expressed, and purified as previously described (2,28). Protein was cocrystallized with either 2 mM CYC or 2 mM PYR in the presence of NADPH and dUMP.…”
Section: Methodsmentioning
confidence: 99%
“…Preparation of recombinant PfDHFR-TS bifunctional enzymes was carried out as previously reported (4). Crystals were flash-frozen in liquid nitrogen by dipping for 10 s in a corresponding crystallization solution containing 20% glycerol as a cryoprotectant.…”
Section: Methodsmentioning
confidence: 99%