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Acta Crystallographica Section F-structural Biology and Crystallization Communications
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#1Eric J. Montemayor (UW: University of Wisconsin-Madison)H-Index: 7
#2Johanna M. Virta (UW: University of Wisconsin-Madison)
Last.Samuel E. Butcher (UW: University of Wisconsin-Madison)H-Index: 36
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The structure of a 22-base-pair RNA helix with mismatched pyrimidine base pairs is reported. The helix contains two symmetry-related CUG sequences: a triplet-repeat motif implicated in myotonic dystrophy type 1. The CUG repeat contains a U–U mismatch sandwiched between Watson–Crick pairs. Additionally, the center of the helix contains a dimerized UUCG motif with tandem pyrimidine (U–C/C–U) mismatches flanked by U–G wobble pairs. This region of the structure is significantly different from previo...
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#1Deanna Dahlke Ojennus (Whitworth University)
#2Nicholas J. Bratt (Whitworth University)
Last.Douglas H. Juers (Whitman College)H-Index: 17
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#1Sonja Schüssler (UHH: University of Hamburg)
#2Ilka Haase (UHH: University of Hamburg)H-Index: 20
Last.Tobias Gräwert (UHH: University of Hamburg)H-Index: 16
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A putative open reading frame encoding GTP cyclohydrolase I from Listeria monocytogenes was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified and was confirmed to convert GTP to dihydroneopterin triphosphate (Km = 53 µM; vmax = 180 nmol mg−1 min−1). The protein was crystallized from 1.3 M sodium citrate pH 7.3 and the crystal structure was solved at a resolution of 2.4 A (Rfree = 0.226) by molecular replacement using human GTP cyclohydrolase I as a template...
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#1Karthik S. Paithankar (Goethe University Frankfurt)H-Index: 7
#2Mathias Enderle (Goethe University Frankfurt)H-Index: 2
Last.Dieter Oesterhelt (MPG: Max Planck Society)H-Index: 82
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Archaea are motile by the rotation of the archaellum. The archaellum switches between clockwise and counterclockwise rotation, and movement along a chemical gradient is possible by modulation of the switching frequency. This modulation involves the response regulator CheY and the archaellum adaptor protein CheF. In this study, two new crystal forms and protein structures of CheY are reported. In both crystal forms, CheY is arranged in a domain-swapped conformation. CheF, the protein bridging the...
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#1Babak Andi (BNL: Brookhaven National Laboratory)H-Index: 5
#2Alexei S. Soares (BNL: Brookhaven National Laboratory)H-Index: 16
Last.Qun Liu (BNL: Brookhaven National Laboratory)H-Index: 29
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The crystallization of amidase, the ultimate enzyme in the Trp-dependent auxin-biosynthesis pathway, from Arabidopsis thaliana was attempted using protein samples with at least 95% purity. Cube-shaped crystals that were assumed to be amidase crystals that belonged to space group I4 (unit-cell parameters a = b = 128.6, c = 249.7 A) were obtained and diffracted to 3.0 A resolution. Molecular replacement using structures from the PDB containing the amidase signature fold as search models was unsucc...
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#1M. Takenoya (Tokyo University of Agriculture)H-Index: 2
#2Tatsuro Shimamura (Kyoto University)H-Index: 23
Last.Shunsuke Yajima (Tokyo University of Agriculture)H-Index: 20
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Hygromycin B (HygB) is one of the aminoglycoside antibiotics, and it is widely used as a reagent in molecular-biology experiments. Two kinases are known to inactivate HygB through phosphorylation: aminoglycoside 7′′-phosphotransferase-Ia [APH(7′′)-Ia] from Streptomyces hygroscopicus and aminoglycoside 4-phosphotransferase-Ia [APH(4)-Ia] from Escherichia coli. They phosphorylate the hydroxyl groups at positions 7′′ and 4 of the HygB molecule, respectively. Previously, the crystal structure of APH...
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