title: Crystallization of the complex of actin with gelsolin segment 1.
abstract: Crystals of a 1:1 complex between human gelsolin segment 1 and actin have been grown from solutions containing polyethylene glycol 6000. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 57.4 A, b = 70.4 A, c = 184.5 A. They are moderately stable to X-rays and diffract to beyond 2.5 A. There is one molecule of complex in the asymmetric unit.
authors.affiliation: M RC Laboratory of Molecular Biology, Cambridge, England.
authors.forename: H G
authors.initials: HG
authors.lastname: Mannherz
authors.forename: J
authors.initials: J
authors.lastname: Gooch
authors.forename: M
authors.initials: M
authors.lastname: Way
authors.forename: A G
authors.initials: AG
authors.lastname: Weeds
authors.forename: P J
authors.initials: PJ
authors.lastname: McLaughlin
mesh_terms: D000199:Actins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018260:Gelsolin; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011092:Polyethylene Glycols; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D012996:Solutions; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D002135:Calcium-Binding Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012996:Solutions; D011092:Polyethylene Glycols