Structure break resolution easily

Aug 6th, 2022
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How to structure break resolution

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whats going on guys i hope youre doing well now in this video i want to talk about how you can qualify how you can basically decide and calculate not calculate that sounds really mathematical but like just decide how strong a particular break is a break of structure and i want to talk to you about the kind of the small nuances and what i look for and just a simple two-step process pretty much um so yeah so if youre interested in that interesting about how to you know spot a false break etc all of that fun stuff then this will probably be the video for you but first of all my name is sam i hope struggling traders break through to consistency in the description box below theres an application for one-on-one coaching that is very exclusive not many people get through to that so apply only if youre serious but everybody else psycho effects academy is what i recommend its where i share my analysis weekly analysis daily sometimes and uh yeah everything from strategy psychology the inf

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The term atomic resolution was defined a long time ago and it is generally accepted to correspond to an electron-density map (or a map calculated using another type of data, for example nuclear density) in which individual atoms can be distinguished.
Whereas the majority of the solved protein structures are still at resolutions of 34 , a growing number are in the 23 range, and a few are at a resolution better than 2 . The current record is a 1.54 resolution structure (EMD-9865) of apoferritin3.
Apoferritin is commonly used as a benchmark for cryo-EM, because its molecular stability and 24-fold symmetry allow high-resolution reconstructions from relatively few particles.
This sustained team effort led to an unprecedented 1.7 resolution GABAA receptor structure. This was the best reported resolution achieved using cryo-EM for any protein sample other than for the protein apoferritin.
At resolutions of around 4 , a main-chain tracing method13,14, such as MAINMAST15,16, can be applied for modeling. For maps of resolution between 5 and 8 , some fragments of the secondary structure of proteins are typically visible, but a full trace of the main chain is very difficult to obtain.
What is normally referred to as resolution is the nominal resolution ( d h i g h ). This is defined by the smallest distance (typically measured in ) between crystal lattice planes that is resolved in the diffraction pattern, i.e., if this number is lower, the resolution is higher and vice versa.
Resolution, in structure determinations, is the distance corresponding to the smallest observable feature: if two objects are closer than this distance, they appear as one combined blob rather than two separate objects.
In protein X-ray crystallography, resolution is often used as a good indicator of structural quality. Diffraction resolution of protein crystals correlates well with the number of X-ray observables that are used in structure generation and, therefore, with protein coordinate errors.

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