Abstract
One of the most frequent problems in crystallization is poor quality of the crystals. In order to overcome this obstacle several methods have been utilized, including amino-acid substitutions of the target protein. Here, an example is presented of crystal-quality improvement by leucine-to-methionine substitutions. A variant protein with three amino-acid substitutions enabled improvement of the crystal quality of the histone chaperone SET/TAF-Ibeta/INHAT when combined with optimization of the cryoconditions. This procedure improved the resolution of the SET/TAF-Ibeta/INHAT crystals from around 5.5 to 2.3 A without changing the crystallization conditions.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Substitution
-
Chromosomal Proteins, Non-Histone / chemistry
-
Chromosomal Proteins, Non-Histone / genetics*
-
Chromosomal Proteins, Non-Histone / metabolism
-
Crystallization
-
Crystallography, X-Ray
-
DNA-Binding Proteins
-
Genetic Variation
-
Histone Chaperones
-
Histones / metabolism
-
Humans
-
Leucine / metabolism*
-
Methionine / metabolism*
-
Molecular Chaperones / chemistry
-
Molecular Chaperones / genetics*
-
Molecular Chaperones / metabolism
-
Sensitivity and Specificity
-
Transcription Factors / chemistry
-
Transcription Factors / genetics*
-
Transcription Factors / metabolism
Substances
-
Chromosomal Proteins, Non-Histone
-
DNA-Binding Proteins
-
Histone Chaperones
-
Histones
-
Molecular Chaperones
-
SET protein, human
-
Transcription Factors
-
Methionine
-
Leucine