Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungusTrichoderma longibrachiatum
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چکیده
منابع مشابه
Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.
A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4×1.3×0.7 mm (3.6 mm3) in size was obtained by sequential application of microseeding and macroseeding. A neutron diffraction data set was collected to 2.0 Å resolution using the IMAGINE diffractometer at the High Flux Isotope Reactor within Oak Ridge National Laboratory. A 1.6 Å resolution X-ray d...
متن کاملCrystallization and preliminary X-ray crystallographic studies of the PDZ domain of Shank1 from Rattus norvegicus.
Shank proteins are a new family of scaffold proteins interacting with various membrane and cytoplasmic proteins. Shank contains multiple protein-protein interaction sites, including ankyrin repeats, an SH3 domain, a PDZ domain, a long proline-rich region and an SAM domain. The PDZ domain of Shank binds to the C-terminus of guanylate kinase-associated protein (GKAP). The PDZ domain of Shank1 fro...
متن کاملCrystallization and preliminary X-ray crystallographic studies of the ice-binding protein from the Antarctic yeast Leucosporidium sp. AY30. Corrigendum
Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136713, Republic of Korea, Division of Polar Biology and Ocean Sciences, Korea Polar Research Institute, Incheon 406-840, Republic of Korea, University of Science and Technology (UST), Yuseong-gu, Daejeon 305-333, Republic of Korea, and Institute of Life Sciences and Natural Resources, Korea University, Seoul 136-713, ...
متن کاملBinding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein
Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit the enhanced visibility of isotopically replaced hydrogen atoms, yield new information on the stability of the protein and the possible mechanisms ...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2011
ISSN: 1744-3091
DOI: 10.1107/s174430911005075x