Crystals: Difference between revisions
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== Crystal Characterization == | == Crystal Characterization == | ||
* [[Birefringence]] | * [[Birefringence]] | ||
* [[solvent content]] | |||
== Crystal Imperfections == | == Crystal Imperfections == | ||
* [[Diffuse Scattering]] | * [[Diffuse Scattering]] | ||
* [[Incommensurate Lattices]] | * [[Incommensurate Lattices]] | ||
* [[Examples of diffraction patterns showing particular features]] | |||
== Crystal Growth == | == Crystal Growth == | ||
| Line 13: | Line 15: | ||
* [[Conditions prone to salt crystallization]] | * [[Conditions prone to salt crystallization]] | ||
* [[Biophysical methods]] for evaluation of crystallization tendency | * [[Biophysical methods]] for evaluation of crystallization tendency | ||
* [[Improving crystal quality]] | |||
* [[Robots for crystallization setup]] | * [[Robots for crystallization setup]] | ||
* [[Visualization of crystal growth]] | * [[Visualization of crystal growth]] | ||
| Line 19: | Line 22: | ||
* [[Robots for crystallization monitoring]] | * [[Robots for crystallization monitoring]] | ||
* [[Crystal growth: Tips and Tricks]] | * [[Crystal growth: Tips and Tricks]] | ||
* [[Crystal growth: Protein-DNA complexes]] | |||
* [[BMCD|Biomolecular crystallization database]] | |||
* Prediction of protein crystallizability: [http://ffas.burnham.org/XtalPred-cgi/xtal.pl XtalPred] | |||
* crystallization of soluble proteins (see also [[Improving crystal quality]]) | |||
* crystallization of membrane proteins (see also [[Improving crystal quality#Improving diffraction quality of membrane protein crystals]]) | |||
* relative humidity calculations of salt/PEG solutions - can also be used to calculate equivalent/matching osmotic pressure: http://go.esrf.eu/RH | |||
== Crystal handling == | == Crystal handling == | ||
* [[Cryo]] | |||
* [[Sticky crystals]] | * [[Sticky crystals]] | ||
* [[Soaking with heavy atoms]] | |||
* [[Microseeding]] | |||
== Data collection == | == Data collection == | ||
* [[X-ray generators | * [[X-ray generators]] | ||
* [[Detectors]] | |||
* [[Synchrotrons]] | * [[Synchrotrons]] | ||
* [[Strategies]] | * [[Strategies]] | ||
* [[Data quality]] | * [[Data quality]] | ||
* [[Radiation damage]] | * [[Radiation damage]] | ||
* [[some ways to calculate the radiation dose that a crystal has absorbed]] | |||
* [[Comparison of home source and synchrotron properties]] | |||
* [[Data collection: Tips and Tricks]] | * [[Data collection: Tips and Tricks]] | ||
* [[Storage of diffraction data]] | |||
== References == | == References == | ||
# Wiener MC (2004) A pedestrian guide to membrane protein crystallization. Methods 34(3), 364-372. | # Wiener MC (2004) A pedestrian guide to membrane protein crystallization. Methods 34(3), 364-372. | ||
# Loll PJ (2003) Membrane protein structural biology: the high throughput challenge. J. Struct. Biol. 142(1), 144-153. | # Loll PJ (2003) Membrane protein structural biology: the high throughput challenge. J. Struct. Biol. 142(1), 144-153. | ||
| Line 42: | Line 54: | ||
# Macromolecular Crystallography Protocols, Volume 1: Preparation and Crystallization of Macromolecules. Doublie S (Ed.), Totowa, NJ: Humana Press. (2007) | # Macromolecular Crystallography Protocols, Volume 1: Preparation and Crystallization of Macromolecules. Doublie S (Ed.), Totowa, NJ: Humana Press. (2007) | ||
# Structural Biology of Membrane Proteins. Grisshammer R, & Buchanan SK (Eds.), Cambridge, UK: Royal Society of Chemistry. (2006) | # Structural Biology of Membrane Proteins. Grisshammer R, & Buchanan SK (Eds.), Cambridge, UK: Royal Society of Chemistry. (2006) | ||
# Macromolecular Crystallisation and Crystal Perfection. N E Chayen, J R Helliwell and E H Snell OUP 2010 [http://www.oxfordscholarship.com/oso/public/content/physics/9780199213252/toc.html] | |||
Latest revision as of 08:56, 19 June 2020
Crystal Characterization[edit | edit source]
Crystal Imperfections[edit | edit source]
- Diffuse Scattering
- Incommensurate Lattices
- Examples of diffraction patterns showing particular features
Crystal Growth[edit | edit source]
- Modifying the protein to crystallize better
- Crystallization screens and methods
- I have crystals, but are they salt?
- Conditions prone to salt crystallization
- Biophysical methods for evaluation of crystallization tendency
- Improving crystal quality
- Robots for crystallization setup
- Visualization of crystal growth
- Crystal mounting
- Robots for crystal mounting
- Robots for crystallization monitoring
- Crystal growth: Tips and Tricks
- Crystal growth: Protein-DNA complexes
- Biomolecular crystallization database
- Prediction of protein crystallizability: XtalPred
- crystallization of soluble proteins (see also Improving crystal quality)
- crystallization of membrane proteins (see also Improving crystal quality#Improving diffraction quality of membrane protein crystals)
- relative humidity calculations of salt/PEG solutions - can also be used to calculate equivalent/matching osmotic pressure: http://go.esrf.eu/RH
Crystal handling[edit | edit source]
Data collection[edit | edit source]
- X-ray generators
- Detectors
- Synchrotrons
- Strategies
- Data quality
- Radiation damage
- some ways to calculate the radiation dose that a crystal has absorbed
- Comparison of home source and synchrotron properties
- Data collection: Tips and Tricks
- Storage of diffraction data
References[edit | edit source]
- Wiener MC (2004) A pedestrian guide to membrane protein crystallization. Methods 34(3), 364-372.
- Loll PJ (2003) Membrane protein structural biology: the high throughput challenge. J. Struct. Biol. 142(1), 144-153.
- Methods and Results in Crystallization of Membrane Proteins Iwata S (Ed.), San Diego, CA: International University Line. (2003)
- Macromolecular Crystallography Protocols, Volume 1: Preparation and Crystallization of Macromolecules. Doublie S (Ed.), Totowa, NJ: Humana Press. (2007)
- Structural Biology of Membrane Proteins. Grisshammer R, & Buchanan SK (Eds.), Cambridge, UK: Royal Society of Chemistry. (2006)
- Macromolecular Crystallisation and Crystal Perfection. N E Chayen, J R Helliwell and E H Snell OUP 2010 [1]