CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE

A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.

147 BP WIDOM 601 DNA FRAGMENT (+ STRAND)

147 BP WIDOM 601 DNA FRAGMENT (- STRAND)

10% MPD, 40MM SODIUM CACODYLATE, 24MM SPERMINE TETRA-HCL, 80MM SODIUM CHLORIDE, 20MM MAGNESIUM CHLORIDE; RESERVIOR 35% MPD. PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K

DNA sequences had errors in 4INM.
DNA sequences are corrected
and coordinates are updated in this entry.

THE DISCREPANCY AT THE C-TERM OF H3 SEQUENCES (CHAINS A,E,K,O) IS A RESULT OF CHIMERIC CENP-A, I.E. THE LAST THREE RESIDUES OF H3 (-ERA) TO THE LAST SIX RESIDUES OF CENP-A (-IEGGLG)

CNS 1.3 WAS USED FOR LOW RESOLUTION REFINEMENT

HISTONE H3/CENP-A, HISTONE H4, HISTONE H2A, HISTONE H2B, VAL-ARG-ARG-SER-ASN-ARG-ILE-ARG-LEU-LYS-PRO-LEU-GLU-TYR-TRP-ARG-GLY-GLU-ARG-ILE-ASP-TYR/DNA Complex

NUCLEOSOME CORE PARTICLE, WIDOM 601 DNA FRAGMMENT, HISTONE FOLD, CENP-C COMPLEX, SEGREGATION, CHROMOSOME CENTROMERE, KINETOCHORE ASSEMBLY, CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK (CCAN) PROTEINS, STRUCTURAL PROTEIN-DNA COMPLEX