Search results
Results from the WOW.Com Content Network
NMR has advantages over X-ray crystallography, which is the other method for high-resolution nucleic acid structure determination, in that the molecules are being observed in their natural solution state rather than in a crystal lattice that may affect the molecule's structural properties. It is also possible to investigate dynamics with NMR.
An advantage of cryo-EM over x-ray crystallography is that the samples are preserved in their aqueous solution state and not perturbed by forming a crystal of the sample. One disadvantage, is that it is difficult to resolve nucleic acid or protein structures that are smaller than ~75 kilodaltons , partly due to the difficulty of having enough ...
A common goal of these investigations is to obtain high resolution 3-dimensional structures of the protein, similar to what can be achieved by X-ray crystallography. In contrast to X-ray crystallography, NMR spectroscopy is usually limited to proteins smaller than 35 kDa, although larger structures have been solved. NMR spectroscopy is often ...
A set of conformations, determined by NMR or X-ray crystallography may be a better representation of the experimental data of a protein than a unique conformation. [23] The utility of a model will be given, at least in part, by the degree of accuracy and precision of the model.
Nuclear magnetic resonance crystallography (NMR crystallography) is a method which utilizes primarily NMR spectroscopy to determine the structure of solid materials on the atomic scale. Thus, solid-state NMR spectroscopy would be used primarily, possibly supplemented by quantum chemistry calculations (e.g. density functional theory ), [ 1 ...
Isomorphous replacement (IR) is historically the most common approach to solving the phase problem in X-ray crystallography studies of proteins.For protein crystals this method is conducted by soaking the crystal of a sample to be analyzed with a heavy atom solution or co-crystallization with the heavy atom.
Figure 2. Histogram of ResProx equivalent resolution for NMR models and experimental resolution for X-ray structures. 500 NMR ensembles and 500 X-ray structures were randomly selected from the PDB. Proteins were grouped in 0.25Å resolution bins. Resolution values on the X-axis indicate the upper limit of each resolution bin.
It is used in the fields of X-ray crystallography and nuclear magnetic resonance spectroscopy of proteins (NMR) analysis. [1] X-PLOR is a highly sophisticated program that provides an interface between theoretical foundations and experimental data in structural biology, with specific emphasis on X-ray crystallography and nuclear magnetic ...