The Ability to Enhance the Solubility of Its Fusion Partners Is an Intrinsic Property of Maltose-Binding Protein but Their Folding Is Either Spontaneous or Chaperone-Mediated

Expression of proteins inEscherichia colias fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline

(2011) Stephen N. Hewitt et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented

(2011) Navneet K. Tyagi et al.   FEBS LETTERS

Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3)

(2011) Brian P. Austin et al.   PROTEIN EXPRESSION AND PURIFICATION

A systematic survey of in vivo obligate chaperonin-dependent substrates

(2010) Kei Fujiwara et al.   EMBO JOURNAL

Overproduction, purification and structure determination of human dual-specificity phosphatase 14

(2009) George T. Lountos et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

High-throughput screening of soluble recombinant proteins

(2002) Yan-Ping Shih et al.   PROTEIN SCIENCE

Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli

(2002) Martin Hammarström et al.   PROTEIN SCIENCE