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pmid: 1138109
The Fab′ fragment of McPC603 mouse myeloma immunoglobulin with phosphorylcholine-binding activity crystallizes into both a hexagonal and a cubic structure. Models of these structures showing approximate molecular packing were deduced from an electron microscopic examination of stained crystal sections, a preliminary X-ray diffraction study, and the knowledge that both crystal structures grow simultaneously in the same crystallizing solution. When both of these models were modified slightly to agree with the more exact molecular packing in the hexagonal crystal from a 4.5 resolution X-ray study, they were both still compatible with the EM data.
Models, Molecular, Protein Conformation, Phosphorylcholine, Choline, Immunoglobulin Fab Fragments, Mice, Microscopy, Electron, X-Ray Diffraction, Animals, Crystallization, Protein Binding
Models, Molecular, Protein Conformation, Phosphorylcholine, Choline, Immunoglobulin Fab Fragments, Mice, Microscopy, Electron, X-Ray Diffraction, Animals, Crystallization, Protein Binding
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 8 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |