X-ray structure of the nucleosome core particle.
Two monoclinic crystal forms (P2(1),C2) of chicken erythrocyte nucleosomes have been under study in this laboratory. The x-ray structure of the P2(1) crystal form has been solved to 15 A resolution. The B-DNA superhelix has a relatively uniform curvature, with only several local distortions observed in the superhelix. The individual histone domains have been localized and specific contacts between each histone and the DNA can be observed. Histone contacts to the inner surface of the DNA superhelix occur predominantly at the minor groove sites. Most of the histone core is contained within the inner surface of the superhelical DNA, except for part of H2A which extends between the DNA gyres near the terminus of the DNA. No part of H2A blocks the DNA terminus or would prevent a smooth exit of the DNA into the linker region. A similar extension of a portion of histone H4 between the DNA gyres occurs close to the dyad axis. Both unique nucleosomes in the P2(1) asymmetric unit demonstrate good dyad symmetry and are similar to each other throughout the histone core and DNA regions.
D000818:Animals; D002645:Chickens / Q000097:blood; D002843:Chromatin / Q000648:ultrastructure; D003460:Crystallization; D004247:DNA / Q000378:metabolism / Q000648:ultrastructure; D004278:DNA, Superhelical; D004912:Erythrocytes / Q000648:ultrastructure*; D006657:Histones / Q000378:metabolism; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000648:ultrastructure*; D014961:X-Ray Diffraction
D002843:Chromatin; D004278:DNA, Superhelical; D006657:Histones; D046911:Macromolecular Substances; D009707:Nucleosomes; D004247:DNA