title: Crystallization and preliminary X-ray diffraction studies of the engrailed homeodomain and of an engrailed homeodomain/DNA complex.
abstract: The homeodomain from the engrailed protein of Drosophila has been crystallized from ammonium phosphate at pH 6.8. The crystals form in space group P6(1)22 (or P6(5)22), with cell dimensions a = b = 44.8 A and c = 118.2 A. These crystals diffract to 1.8 A resolution. A complex containing the engrailed homeodomain and a duplex DNA site also has been crystallized. The cocrystals form in space group C2 with a = 131.2 A, b = 45.5 A, c = 72.9 A and beta = 119.0 degrees. These crystals diffract to 2.6 A resolution.
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
authors.forename: B
authors.initials: B
authors.lastname: Liu
authors.forename: C R
authors.initials: CR
authors.lastname: Kissinger
authors.forename: C O
authors.initials: CO
authors.lastname: Pabo
mesh_terms: D000818:Animals; D001483:Base Sequence; D003461:Crystallography; D003852:Deoxyribonucleoproteins / Q000648:ultrastructure*; D004331:Drosophila melanogaster; D005801:Genes, Homeobox; D008969:Molecular Sequence Data; D012045:Regulatory Sequences, Nucleic Acid; D014961:X-Ray Diffraction
chemical_list: D003852:Deoxyribonucleoproteins