scholarly journals The difference electron-density map as a crystal structure validation tool

2019 ◽  
Vol 75 (a2) ◽  
pp. e756-e756
Author(s):  
Ton Spek
Keyword(s):  
Crystal Structure ◽  
Electron Density ◽  
Structure Validation ◽  
Difference Electron Density ◽  
Density Map ◽  
The Difference ◽  
Electron Density Map ◽  
Validation Tool

The iron content of iron superoxide dismutase: determination by anomalous scattering

1983 ◽  
Vol 218 (1210) ◽  
pp. 119-126 ◽  
Keyword(s):  
Superoxide Dismutase ◽  
Iron Content ◽  
Three Dimensional ◽  
Anomalous Scattering ◽  
Total Iron Content ◽  
Iron Site ◽  
Iron Superoxide Dismutase ◽  
Density Map ◽  
The Difference ◽  
Electron Density Map

The number of iron atoms in the dimeric iron-containing superoxide dismutase from Pseudomonas ovalis and their atomic positions have been determined directly from anomalous scattering measurements on crystals of the native enzyme. To resolve the long-standing question of the total amount of iron per molecule for this class of dismutase, the occupancy of each site was refined against the measured Bijvoet differences. The enzyme is a symmetrical dimer with one iron site in each subunit. The iron position is 9 ņ from the intersubunit interface. The total iron content of the dimer is 1.2±0.2 moles per mole of protein. This is divided between the subunits in the ratio 0.65:0.55; the difference between them is probably not significant. Since each subunit contains, on average, slightly more than half an iron atom we conclude that the normal state of this enzyme is two iron atoms per dimer but that some of the metal is lost during purification of the protein. Although the crystals are obviously a mixture of holo- and apo-enzymes, the 2.9 Å electron density map is uniformly clean, even at the iron site. We conclude that the three-dimensional structures of the iron-bound enzyme and the apoenzyme are identical.

A Comparison of Two Algorithms for Electron-Density Map Improvement by Introduction of Atomicity: Skeletonization, and Map Sorting Followed by Refinement

1998 ◽  
Vol 54 (1) ◽  
pp. 81-85 ◽  
Author(s):  
F. M. D. Vellieux
Keyword(s):  
Electron Density ◽  
Initial Density ◽  
Acta Cryst ◽  
Density Maps ◽  
Resolution Electron ◽  
Crystallographic Symmetry ◽  
Density Map ◽  
Ornithine Transcarbamoylase ◽  
Electron Density Map ◽  
Pseudo Atom

A comparison has been made of two methods for electron-density map improvement by the introduction of atomicity, namely the iterative skeletonization procedure of the CCP4 program DM [Cowtan & Main (1993). Acta Cryst. D49, 148–157] and the pseudo-atom introduction followed by the refinement protocol in the program suite DEMON/ANGEL [Vellieux, Hunt, Roy & Read (1995). J. Appl. Cryst. 28, 347–351]. Tests carried out using the 3.0 Å resolution electron density resulting from iterative 12-fold non-crystallographic symmetry averaging and solvent flattening for the Pseudomonas aeruginosa ornithine transcarbamoylase [Villeret, Tricot, Stalon & Dideberg (1995). Proc. Natl Acad. Sci. USA, 92, 10762–10766] indicate that pseudo-atom introduction followed by refinement performs much better than iterative skeletonization: with the former method, a phase improvement of 15.3° is obtained with respect to the initial density modification phases. With iterative skeletonization a phase degradation of 0.4° is obtained. Consequently, the electron-density maps obtained using pseudo-atom phases or pseudo-atom phases combined with density-modification phases are much easier to interpret. These tests also show that for ornithine transcarbamoylase, where 12-fold non-crystallographic symmetry is present in the P1 crystals, G-function coupling leads to the simultaneous decrease of the conventional R factor and of the free R factor, a phenomenon which is not observed when non-crystallographic symmetry is absent from the crystal. The method is far less effective in such a case, and the results obtained suggest that the map sorting followed by refinement stage should be by-passed to obtain interpretable electron-density distributions.

[3]Rotane: crystal structure, X-X difference electron density, and phase transition

1991 ◽  
Vol 113 (5) ◽  
pp. 1743-1748 ◽  
Author(s):  
Roland Boese ◽  
Thomas Miebach ◽  
Armin De Meijere
Keyword(s):  
Crystal Structure ◽  
Phase Transition ◽  
Electron Density ◽  
Difference Electron Density

Electron-density maps

2002 ◽  
Author(s):  
David Blow
Keyword(s):  
Fourier Transform ◽  
Electron Density ◽  
Three Dimensional ◽  
Two Dimensions ◽  
Unit Cell ◽  
Density Maps ◽  
Wave Cycle ◽  
Density Map ◽  
The Fourier Transform ◽  
Electron Density Map

When everything has been done to make the phases as good as possible, the time has come to examine the image of the structure in the form of an electron-density map. The electron-density map is the Fourier transform of the structure factors (with their phases). If the resolution and phases are good enough, the electron-density map may be interpreted in terms of atomic positions. In practice, it may be necessary to alternate between study of the electron-density map and the procedures mentioned in Chapter 10, which may allow improvements to be made to it. Electron-density maps contain a great deal of information, which is not easy to grasp. Considerable technical effort has gone into methods of presenting the electron density to the observer in the clearest possible way. The Fourier transform is calculated as a set of electron-density values at every point of a three-dimensional grid labelled with fractional coordinates x, y, z. These coordinates each go from 0 to 1 in order to cover the whole unit cell. To present the electron density as a smoothly varying function, values have to be calculated at intervals that are much smaller than the nominal resolution of the map. Say, for example, there is a protein unit cell 50 Å on a side, at a routine resolution of 2Å. This means that some of the waves included in the calculation of the electron density go through a complete wave cycle in 2 Å. As a rule of thumb, to represent this properly, the spacing of the points on the grid for calculation must be less than one-third of the resolution. In our example, this spacing might be 0.6 Å. To cover the whole of the 50 Å unit cell, about 80 values of x are needed; and the same number of values of y and z. The electron density therefore needs to be calculated on an array of 80×80×80 points, which is over half a million values. Although our world is three-dimensional, our retinas are two-dimensional, and we are good at looking at pictures and diagrams in two dimensions.

scholarly journals Crystal structure of d(CCGGGGTACCCCGG)2at 1.4 Å resolution

2017 ◽  
Vol 73 (5) ◽  
pp. 259-265
Author(s):  
Selvam Karthik ◽  
Arunachalam Thirugnanasambandam ◽  
Pradeep Kumar Mandal ◽  
Namasivayam Gautham
Keyword(s):  
Crystal Structure ◽  
Metal Ion ◽  
Double Helix ◽  
Barium Chloride ◽  
Base Pairs ◽  
X Ray ◽  
Density Map ◽  
Solvent Molecules ◽  
Electron Density Map ◽  
Phosphate Groups

The X-ray crystal structure of the DNA tetradecamer sequence d(CCGGGGTACCCCGG)2is reported at 1.4 Å resolution in the tetragonal space groupP41212. The sequence was designed to fold as a four-way junction. However, it forms an A-type double helix in the presence of barium chloride. The metal ion could not be identified in the electron-density map. The crystallographic asymmetric unit consists of one A-type double helix with 12 base pairs per turn, in contrast to 11 base pairs per turn for canonical A-DNA. A large number of solvent molecules have been identified in both the grooves of the duplex and around the backbone phosphate groups.

scholarly journals Electron density map as an aid in the sequencing of peptides.

1973 ◽  
Vol 70 (6) ◽  
pp. 1793-1794 ◽  
Author(s):  
M. J. Adams ◽  
G. C. Ford ◽  
P. J. Lentz ◽  
A. Liljas ◽  
M. G. Rossmann
Keyword(s):  
Electron Density ◽  
Density Map ◽  
Electron Density Map
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