Crystallographic factor

  • What does the crystallographic R factor measure?

    The quality of an X-ray crystal structure is evaluated in several ways, including the 'crystallographic R-factor', which gives a measure of how faithfully the calculated structure represents the experimental data, the X-ray reflections..

  • What is a structure factor in crystallography?

    A structure factor represents the resultant X-ray scattering power of the whole crystal structure, though, since the whole structure consists of a large number of unit cells all scattering in phase with each other, the resultant scattering power is actually calculated for the contents of one unit cell only..

  • What is the R-factor in structural biology?

    R-factor.
    This is a measure of the disagreement between the observed amplitudes (Fo) and the amplitudes calculated from the model (Fc).
    Depending on the resolution and quality of the diffraction data, well-refined structures have R-factors below 20–25 percent..

  • In crystallography, the R-factor (sometimes called residual factor or reliability factor or the R-value or RWork) is a measure of the agreement between the crystallographic model and the experimental X-ray diffraction data.
    In other words, it is a measure of how well the refined structure predicts the observed data.
  • R -factor is a formula for estimating errors in a data set.
    It is usually the sum of the absolute difference between observed (Fo) and calculated (Fc) over the sum of the observed: (3..
    1. R crystallographic = ∑ F o - F c ∑ F o
  • R-value is the measure of the quality of the atomic model obtained from the crystallographic data.
    When solving the structure of a protein, the researcher first builds an atomic model and then calculates a simulated diffraction pattern based on that model.
In crystallography, the R-factor is a measure of the agreement between the crystallographic model and the experimental X-ray diffraction data. In other words, it is a measure of how well the refined structure predicts the observed data. Wikipedia
Crystallographic factor
Crystallographic factor
Anthrax lethal factor endopeptidase is an enzyme that catalyzes the hydrolysis of mitogen-activated protein kinase kinases.
This enzyme is a component of the lethal factor produced by the bacterium Bacillus anthracis.
The preferred cleavage site can be denoted by BBBBxHxH, in which B denotes a basic amino acid Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid.
Apoptosis inducing factor is involved in initiating a caspase-

Apoptosis inducing factor is involved in initiating a caspase-

Protein family

Apoptosis inducing factor is involved in initiating a caspase-independent pathway of apoptosis by causing DNA fragmentation and chromatin condensation.
Apoptosis inducing factor is a flavoprotein.
It also acts as an NADH oxidase.
Another AIF function is to regulate the permeability of the mitochondrial membrane upon apoptosis.
Normally it is found behind the outer membrane of the mitochondrion and is therefore secluded from the nucleus.
However, when the mitochondrion is damaged, it moves to the cytosol and to the nucleus.
Inactivation of AIF leads to resistance of embryonic stem cells to death following the withdrawal of growth factors indicating that it is involved in apoptosis.

Categories

Crystallography structure factor
Crystallography reports impact factor
Scattering factor crystallography
Garnet crystallography
Crystallography of galena
Law of symmetry in crystallography
Crystallography habit plane definition
Crystallography habit plane
Hampton crystallography
Harvard crystallography
Hammond crystallography
Handedness crystallography
Crystallographic habit planes
Crystallography of halite
Crystallography crystal habit
Cc half crystallography
Crystallography math ia
Michael james crystallography
Crystallography of jarosite
Crystallography lattice planes