Talk:Resolution: Difference between revisions

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==ARTICLE REVISED JUNE 15, 2014==
I incorporated most of the suggestions below into a major revision of the article.
[[User:Eric Martz|Eric Martz]] 02:02, 16 June 2014 (IDT)
==Proposed revision V2==
==Proposed revision V2==
In structure determinations, resolution is the distance corresponding to the smallest observable feature, i.e. if two objects are closer than this distance, they appear as one combined blob rather than two separate objects. For example, because the resolution of the light microscope is limited to roughly the wave length of light (400 nm = 4000 Å), it is not possible to resolve ("see") separate atoms under a microscope (atomic distances are on the order of 1 Å). The resolution of X-ray crystallography is theoretically limited by the wave length of X-rays (also on the order of 1 Å), but in practice, the quality of the available crystals determines resolution. High numeric values of resolution, such as 4 Å, mean poor resolution, while low numeric values, such as 1.5 Å, mean good resolution. A structure determined using data to 1.5 Å would be referred to as a "1.5 Å structure". 2.05 Å is the median resolution for X-ray crystallographic results in the Protein Data Bank (88,701 on May 15, 2014).
In structure determinations, resolution is the distance corresponding to the smallest observable feature, i.e. if two objects are closer than this distance, they appear as one combined blob rather than two separate objects. For example, because the resolution of the light microscope is limited to roughly the wave length of light (400 nm = 4000 Å), it is not possible to resolve ("see") separate atoms under a microscope (atomic distances are on the order of 1 Å). The resolution of X-ray crystallography is theoretically limited by the wave length of X-rays (also on the order of 1 Å), but in practice, the quality of the available crystals determines resolution. High numeric values of resolution, such as 4 Å, mean poor resolution, while low numeric values, such as 1.5 Å, mean good resolution. A structure determined using data to 1.5 Å would be referred to as a "1.5 Å structure". 2.05 Å is the median resolution for X-ray crystallographic results in the Protein Data Bank (88,701 on May 15, 2014).