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Structure of a dimeric fragment related to the lambda-type Bence-Jones protein: A preliminary study

Published on Aug 1, 1974in Journal of Molecular Biology5.067
· DOI :10.1016/0022-2836(74)90100-4
Bi-Cheng Wang48
Estimated H-index: 48
,
Martin Sax21
Estimated H-index: 21
Abstract
Abstract A Bence-Jones protein, Rhe, isolated from the urine of a myeloma patient, has been crystallized. Immunological tests indicate that Rhe contains the constant region of a lambda-type light chain. Gel filtration and sodium dodecyl sulfate gel electrophoresis show that Rhe consists of two subunits, each about half the size of the light chain. Preliminary X-ray crystallographic results and density measurements show that Rhe possesses crystallographic 2-fold symmetry, indicating that the two subunits of Rhe are identical. This is the first report of evidence suggesting the possible occurrence in Bence-Jones protein of dinners comprised of solely the constant half of the light chain. Heavy-atom derivatives, possibly useful for a crystal structure analysis, have been prepared.
  • References (7)
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Abstract Sweet potato β-amylase has been crystallized in the tetragonal space group P 4 1 22 (or enantiomorph) with unit cell dimensions a = b = 210.7 A , c = 157.0 A . A new method has been developed by which accurate molecular weight values can be obtained from protein crystals grown from concentrated salt solutions. The method also gives the hydration of the protein in the crystal. Using this new technique the molecular weight of β-amylase was found to be 206,000 ± 10,000. The enzyme is tetra...
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Abstract Forty proteins with polypeptide chains of well characterized molecular weights have been studied by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate following the procedure of Shapiro, Vinuela, and Maizel (Biochem. Biophys. Res. Commun., 28, 815 (1967)). When the electrophoretic mobilities were plotted against the logarithm of the known polypeptide chain molecular weights, a smooth curve was obtained. The results show that the method can be used with great co...
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Abstract An analysis has been made, from the data which are currently available, of the solvent content of 116 different crystal forms of globular proteins. The fraction of the crystal volume occupied by solvent is most commonly near 43 %, but has been observed to have values from about 27 to 65%. In many cases this range will be sufficiently restrictive to enable the probable number of molecules in the crystallographic asymmetric unit to be determined directly from the molecular weight of the p...
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1. Correlation between elution volume, Ve, and molecular weight was investigated for gel filtration of proteins of molecular weights ranging from 3500 (glucagon) to 820000 (α-crystallin) on Sephadex G-200 columns at pH7·5. 2. Allowing for uncertainties in the molecular weights, the results for most of the carbohydrate-free globular proteins fitted a smooth Ve–log(mol.wt.) curve. In the lower part of the molecular-weight range the results were similar to those obtained with Sephadex G-75 and G-10...
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Single crystals of T7 RNA polymerase have been grown to a maximum size of 1.8 × 0.3 × 0.3 mm. The crystals are composed of fully intact T7 RNA polymerase which in enzymatically active upon dissolution. These crystals belong to the monoclinic space group P21 and have unit cell parameters a =114.5 A, b=139.6 A, c=125.7 A, β=98.1° Self-rotation function studies indicate that there are three molecules per asymmetricunit. The crystals diffract to at least 3.0 A resolution. These are the first crystal...
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An enzymatically modified form of bovine neurophysin II has been crystallized in three unique crystal forms. The orthorhombic form crystallizes in space group P21212 with a= 15.33 nm, b= 6.92 nm, c= 3.63 nm, with four molecules in the asymmetric unit. The monoclinic form crystallizes in space group P21 with a= 6.22 nm, b= 9.55 nm, c= 5.45 nm and β= 110.2°, with eight molecules in the asymmetric unit. The tetragonal form crystallizes in space group P41212 or P43212 with a= 14.1 nm and c= 14.2 nm,...
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The crystal structure of Rhe, a λ-type Bence-Jones protein fragment, has been solved and refined to a resolution of 1·6 A. A model fragment consisting of the complete variable domain and the first three residues of the constant domain yields a crystallographic residual R F value of 0·149. The protein exists as a dimer both in solution and in the crystals. Although the “immunoglobulin fold” is generally preserved in the structure, there are significant differences in both the monomer conformation...
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Abstract The crystal structure of protein Rhe, a lambda type V L dimer, has been determined at a resolution of 3 A by the method of multiple isomorphous replacement supplemented with anomalous scattering data. A crystallographic sequence was assigned from an interpretation of the electron density map in an optical comparator and is compared with a chemically determined partial amino acid sequence. The monomeric unit of Rhe, as determined crystallographically, contains 113 amino acids, 110 belong...
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The automated system for interpreting electron density maps of proteins has been applied to a newly calculated map of Bence-Jones protein Rhe. In order to test the methods and criteria incorporated in the program system, interpretation of Rhe was performed independently of the interpretation by Wang et al. (1974, 1975a,b†), who have used classical Richards box techniques. The automated system produced a single polypeptide chain which accounts for the whole molecule. Much of the secondary structu...
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