GCN4-Leucine zipper core mutant as N16A trigonal automatic solution

TB Structural Genomics Consortium (TBSGC)

Automated Protein Crystal Structure Determination Using Elves.

An Engineered Allosteric Switch in Leucine-Zipper Oligomerization

Crystal Structure of an Isoleucine-Zipper Trimer

A Switch between Two-, Three-, and Four-Stranded Coiled Coils in GCN4 Leucine Zipper Mutants

X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil.

Amino acid biosynthesis regulatory protein

100MM BIS-TRIS buffer only, pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 298K

hand-built version of tetragonal crystal form

THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN SACCHAROMYCES CEREVISIAE. THE PROTEIN WAS SYNTHESIZED BY SOLID PHASE PEPTIDE SYNTHESIS.

THIS ENTRY WAS SOLVED USING AUTOMATED STRUCTURE WHILE RELATED ENTRTY 1RB5 WAS SOLVED USING NON-AUTOMATED STRUCTURE DETERMINATION METHOD. THE NUMBER OF CLOSE CONTACTS IN THIS STRUCTURE IS AN ARTIFACT OF THE CURRENT STATE-OF-THE-ART AUTOMATED MODEL BUILDING PROCEDURE.

COILED COIL, LEUCINE ZIPPER, Structural Genomics, TB Structural Genomics Consortium, TBSGC, Activator, Amino-acid biosynthesis, DNA-binding, Nucleus, Phosphoprotein, Transcription, Transcription regulation, DNA BINDING PROTEIN