Richard Avenarius

Krauss, Chiara Russo

doi:10.1007/978-3-030-12637-7_2

Cited by 1 publication

(1 citation statement)

References 11 publications

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“…This is sometimes revealed by disappearing protein crystals upon ligand addition. Increasing the precipitant concentration can counteract this increase in protein solubility and help to maintain diffraction of the crystal after soaking, and in some cases, effectively through crystal dehydration, improve resolution (Russo Krauss et al, 2012). When salt is used as the major precipitant in the crystallization, high concentrations can decrease solubility, especially for hydrophobic ligands, and also cause issues for cryoprotection.…”

Section: Soakingmentioning

confidence: 99%

Guidelines for the successful generation of protein–ligand complex crystals

Müller

2017

Acta Crystallogr D Struct Biol

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With continuous technical improvements at synchrotron facilities, datacollection rates have increased dramatically. This makes it possible to collect diffraction data for hundreds of protein-ligand complexes within a day, provided that a suitable crystal system is at hand. However, developing a suitable crystal system can prove challenging, exceeding the timescale of data collection by several orders of magnitude. Firstly, a useful crystallization construct of the protein of interest needs to be chosen and its expression and purification optimized, before screening for suitable crystallization and soaking conditions can start. This article reviews recent publications analysing large data sets of crystallization trials, with the aim of identifying factors that do or do not make a good crystallization construct, and gives guidance in the design of an expression construct. It provides an overview of common protein-expression systems, addresses how ligand binding can be both help and hindrance for protein purification, and describes ligand co-crystallization and soaking, with an emphasis on troubleshooting.

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Section: Soakingmentioning

confidence: 99%

Guidelines for the successful generation of protein–ligand complex crystals

Müller

2017

Acta Crystallogr D Struct Biol

View full text Add to dashboard Cite

show abstract

Richard Avenarius

Cited by 1 publication

References 11 publications

Guidelines for the successful generation of protein–ligand complex crystals

Guidelines for the successful generation of protein–ligand complex crystals

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