Literature DB >> 3759969

Crystallization of Acanthamoeba profilin-I.

K A Magnus, E E Lattman, M Sato, T D Pollard.   

Abstract

Profilin-I, a protein that inhibits actin polymerization in Acanthamoeba castellanii, has been crystallized in a form suitable for high resolution x-ray analysis. The crystals have the symmetry of the space group C2 with lattice constants a = 110.4 +/- 0.2, b = 31.7 +/- 0.1, c = 33.5 +/- 0.1 A, beta = 112.2 degrees. They diffract to at least 2.0-A resolution. The asymmetric unit contains one 12,800-dalton monomer of profilin-I.

Entities:  

Mesh：

Substances：

Year:  1986        PMID： 3759969

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  2 in total

1.  Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome.

Authors:  D J Kwiatkowski; L Aklog; D H Ledbetter; C C Morton
Journal:  Am J Hum Genet       Date:  1990-03       Impact factor: 11.025

2.  Three-dimensional solution structure of Acanthamoeba profilin-I.

Authors:  V K Vinson; S J Archer; E E Lattman; T D Pollard; D A Torchia
Journal:  J Cell Biol       Date:  1993-09       Impact factor: 10.539
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.