2ob1
ppm1 with 1,8-ANS
Structural highlights
FunctionLCMT1_YEAST Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA technique is described whereby the addition of low concentrations (millimolar to micromolar) of the fluorescent dye 1,8-ANS to the protein solution prior to crystallization results in crystallization experiments in which protein crystals are strongly contrasted above background artifacts when exposed to low-intensity UV radiation. As 1,8-ANS does not covalently modify the protein sample, no further handling or purification steps are necessary. The system has been tested on a wide variety of protein samples and it has been shown that the addition of 1,8-ANS has no discernible effect on the crystallization frequencies or crystallization conditions of these proteins. As 1,8-ANS interacts with a wide variety of proteins, this is proposed to be a general solution for the automated classification of protein crystallization images and the detection of protein crystals. The results also demonstrate the expected discrimination between salt and protein crystals, as well as allowing the straightforward identification of small crystals that grow in precipitate or under a protein skin. A method for the general identification of protein crystals in crystallization experiments using a noncovalent fluorescent dye.,Groves MR, Muller IB, Kreplin X, Muller-Dieckmann J Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):526-35. Epub 2007, Mar 16. PMID:17372358[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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