X-ray crystallography: Difference between revisions
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X-ray crystallography is basically a technique that is usually used to detemine the [[Proteins|three-dimensional structure]] structure of a protein molecule. This technique involves a beam of collimated or parallel X-rays, which is aimed at a crystal of protein molecules. the X-rays are diffracted by the electrons in the crystal, which are(i.e | [[X-ray|X-ray]] crystallography is basically a technique that is usually used to detemine the [[Proteins|three-dimensional structure]] structure of a [[protein|protein]] [[molecule|molecule]]. This technique involves a beam of collimated or parallel [[X-ray|X-rays]], which is aimed at a crystal of protein molecules. the X-rays are diffracted by the [[electron|electrons]] in the crystal, which are (i.e. [[electron|electrons]]) then recorded on film or by an electronic detector and an image of the electron clouds sorrounding atoms in the crystal is produces by the mathematical analysis of the diffraction pattern<ref>Horton, Moran, Scrimgeour, Perry and Rawn(2006)Principles of Biochemistry,4th edition,USA: Pearson Education Inc.</ref>. | ||
X-ray crystallography can also be used to an extent to observe the [[Atoms|atomic]] rearrangements that take place during [[Catalysis|catalysis]] because protein crystals are mostly solvent, their native structures are preserved in the crystalline state and their [[Catalysis|catalytic]] functions also remain intact<ref>Donald Voet, Judith G.Voet and Charlotte W.Pratt(2008)Principles of Biochemistry, 3rd edition,Asia: John Willey and Sons, Inc.</ref>. | X-ray crystallography can also be used to an extent to observe the [[Atoms|atomic]] rearrangements that take place during [[Catalysis|catalysis]] because protein crystals are mostly solvent, their native structures are preserved in the crystalline state and their [[Catalysis|catalytic]] functions also remain intact<ref>Donald Voet, Judith G.Voet and Charlotte W.Pratt(2008)Principles of Biochemistry, 3rd edition,Asia: John Willey and Sons, Inc.</ref><ref>Horton, Moran, Scrimgeour, Perry and Rawn(2006)Principles of Biochemistry, 4th edition, USA: Pearson Education, Inc.</ref><ref>Donald Voet, Judith G. Voet and Charlotte W. Pratt(2008)Principles of Biochemistry, 3rd edition, Asia: John Wiley and Sons, Inc.</ref>. | ||
=== References === | |||
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Latest revision as of 11:13, 1 December 2012
X-ray crystallography is basically a technique that is usually used to detemine the three-dimensional structure structure of a protein molecule. This technique involves a beam of collimated or parallel X-rays, which is aimed at a crystal of protein molecules. the X-rays are diffracted by the electrons in the crystal, which are (i.e. electrons) then recorded on film or by an electronic detector and an image of the electron clouds sorrounding atoms in the crystal is produces by the mathematical analysis of the diffraction pattern[1].
X-ray crystallography can also be used to an extent to observe the atomic rearrangements that take place during catalysis because protein crystals are mostly solvent, their native structures are preserved in the crystalline state and their catalytic functions also remain intact[2][3][4].
References
- ↑ Horton, Moran, Scrimgeour, Perry and Rawn(2006)Principles of Biochemistry,4th edition,USA: Pearson Education Inc.
- ↑ Donald Voet, Judith G.Voet and Charlotte W.Pratt(2008)Principles of Biochemistry, 3rd edition,Asia: John Willey and Sons, Inc.
- ↑ Horton, Moran, Scrimgeour, Perry and Rawn(2006)Principles of Biochemistry, 4th edition, USA: Pearson Education, Inc.
- ↑ Donald Voet, Judith G. Voet and Charlotte W. Pratt(2008)Principles of Biochemistry, 3rd edition, Asia: John Wiley and Sons, Inc.