The detection of sub‐units within the crystallographic asymmetric unit
01 Jan 1962-Acta Crystallographica (International Union of Crystallography (IUCr))-Vol. 15, Iss: 1, pp 24-31
TL;DR: In this article, Rossmann and Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone, and the effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.
Abstract: In this paper, Rossmann & Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone. The effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.
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TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
Abstract: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.
3,482 citations
Book•
01 Jan 1992
TL;DR: This manual to X-PLOR Version 3.1 presents the theoretical background, syntax and function of the programme and also provides a comprehensive list of references and sample input files with comments.
Abstract: X-PLOR is a highly sophisticated computer program that provides an interface between theoretical foundations and experimental data in structural biology, with specific emphasis on X-ray crystallography and nuclear magnetic resonance spectroscopy in solution of large biological macro-molecules. This manual to X-PLOR Version 3.1 presents the theoretical background, syntax, and function of the program and also provides a comprehensive list of references and sample input files with comments. It is intended primarily for researchers and students in the fields of computational chemistry, structural biology, and computational molecular biology.
3,449 citations
TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Abstract: Publisher Summary This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin. The most outstanding property of albumin is its ability to bind reversibly an incredible variety of ligands. The sequences of all albumins are characterized by a unique arrangement of disulfide double loops that repeat as a series of triplets. Albumin belongs to a multigene family of proteins that includes α- fetoprotein (AFP) and vitamin D-binding protein (VDP), also known as G complement (Gc) protein. Although AFP is considered the fetal counterpart of albumin, its binding properties are distinct and it is suggested that AFP may have a higher affinity for some unknown ligands important for fetal development. Domain structure and the arrangement of the disulfides, the surface charge distribution, and the conformational flexibility of the albumin molecule are described. The nature of ligand binding, including small organics, long-chain fatty acids, and metals, to multiple sites on the albumin molecule is clearly depicted. The chapter concludes with the perceptive comments on future directions being taken to explore the structure and function of this fascinating protein.
2,988 citations
TL;DR: Four case studies in using maximum-likelihood molecular replacement, as implemented in the program Phaser, to solve structures of protein complexes are described.
Abstract: Molecular replacement (MR) generally becomes more difficult as the number of components in the asymmetric unit requiring separate MR models (i.e. the dimensionality of the search) increases. When the proportion of the total scattering contributed by each search component is small, the signal in the search for each component in isolation is weak or non-existent. Maximum-likelihood MR functions enable complex asymmetric units to be built up from individual components with a `tree search with pruning' approach. This method, as implemented in the automated search procedure of the program Phaser, has been very successful in solving many previously intractable MR problems. However, there are a number of cases in which the automated search procedure of Phaser is suboptimal or encounters difficulties. These include cases where there are a large number of copies of the same component in the asymmetric unit or where the components of the asymmetric unit have greatly varying B factors. Two case studies are presented to illustrate how Phaser can be used to best advantage in the standard `automated MR' mode and two case studies are used to show how to modify the automated search strategy for problematic cases.
1,533 citations
Cites background from "The detection of sub‐units within t..."
...…is identified by the agreement between the calculated and observed structure factors, measured by one of a number of different MR search functions (e.g. Rossmann & Blow, 1962; Crowther, 1972; Fujinaga & Read, 1987; Navaza & Vernoslova, 1995; Read, 2001; Storoni et al., 2004; McCoy et al., 2005)....
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TL;DR: The first atomic resolution structure of an animal virus, human rhinovirus 14, strikingly similar to known icosahedral plant RNA viruses, and four neutralizing immunogenic regions have been identified.
Abstract: We report the first atomic resolution structure of an animal virus, human rhinovirus 14. It is strikingly similar to known icosahedral plant RNA viruses. Four neutralizing immunogenic regions have been identified. These, and corresponding antigenic sequences of polio and foot-and-mouth disease viruses, reside on external protrusions. A large cleft on each icosahedral face is probably the host cell receptor binding site.
1,347 citations
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