Editing Protein tertiary structure (section)

== Determination ==
The knowledge of the tertiary structure of soluble [[globular protein]]s is more advanced than that of [[membrane protein]]s because the former are easier to study with available technology.

=== X-ray crystallography ===
[[X-ray crystallography]] is the most common tool used to determine [[protein structure]]. It provides high resolution of the structure but it does not give information about protein's [[Protein dynamics|conformational flexibility]].

=== NMR ===
[[Protein NMR]] gives comparatively lower resolution of protein structure. It is limited to smaller proteins. However, it can provide information about conformational changes of a protein in solution.

=== Cryogenic electron microscopy ===
[[Cryogenic electron microscopy]] (cryo-EM) can give information about both a protein's tertiary and quaternary structure. It is particularly well-suited to large proteins and [[Protein complex|symmetrical complexes]] of [[protein subunit]]s.

=== Dual polarisation interferometry ===
[[Dual polarisation interferometry]] provides complementary information about surface captured proteins. It assists in determining structure and conformation changes over time.