Surface engineering of proteins can be a powerful technique for dealing with proteins that yield no or poorly diffracting crystals. In particularly, reductive methylation of proteins has emerged as a standard procedure in several large scale facilities and research programs, i.e. the Midwest Centre of Structural genomics [1] and the Structural Proteomics In Europe (SPINE) program [2,3].

The JBS Methylation Kit is designed for selective methylation of lysine residues. The method does not require laborious cloning/expression/purification but chemically replaces the protons of the amino group of all lysine residues with methyl groups. The result is a surface-engineered protein within 24 hours ready for crystallization.

Each JBScreen Methylation Kit contains all necessary reagents for six methylation experiments. All components are provided ready for use. Just follow the manual step-by-step. No background in chemistry necessary.

[1] Kim et al. (2008) Large-scale evaluation of protein reductive methylation for improving protein crystallization. Nature Methods 5:853.
[2] Fogg et al. (2006) Application of the use of high-throughput technologies to the determination of protein structures of bacterial and viral pathogens. Acta Cryst. D 62:1196.
[3] Walter et al. (2006) Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14:1617.

• Koval et al. (2013) Plant multifunctional nuclease TBN1 with unexpected phospholipase activity: structural study and reaction-mechanism analysis. Acta Cryst. D 69:213.
• Reeks et al. (2013) Structure of a dimeric crenarchaeal Cas6 enzyme with an atypical active site for CRISPR RNA processing. Biochemical Journal DOI: 10.1042/BJ20130269.
• Cima et al. (2012) Insight on an Arginine Synthesis Metabolon from the Tetrameric Structure of Yeast Acetylglutamate Kinase. PLOS one 7:e34734.
• Shi et al. (2006) Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase. Acta Cryst. D 62:1218.

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