Open AccessCrystallization and preliminary X‐ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragment
Author(s) -
Sugiyama Shigeru,
Nomura Yusuke,
Sakamoto Taiichi,
Kitatani Tomoya,
Kobayashi Asako,
Miyakawa Shin,
Takahashi Yoshinori,
Adachi Hiroaki,
Takano Kazufumi,
Murakami Satoshi,
Inoue Tsuyoshi,
Mori Yusuke,
Nakamura Yoshikazu,
Matsumura Hiroyoshi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108028236
Subject(s) - aptamer , rna , orthorhombic crystal system , dna , chemistry , microbiology and biotechnology , antibody , molecule , immunoglobulin fab fragments , crystallography , biology , biochemistry , crystal structure , genetics , immunoglobulin light chain , gene , organic chemistry , complementarity determining region
Aptamers, which are folded DNA or RNA molecules, bind to target molecules with high affinity and specificity. An RNA aptamer specific for the Fc fragment of human immunoglobulin G (IgG) has recently been identified and it has been demonstrated that an optimized 24‐nucleotide RNA aptamer binds to the Fc fragment of human IgG and not to other species. In order to clarify the structural basis of the high specificity of the RNA aptamer, it was crystallized in complex with the Fc fragment of human IgG1. Preliminary X‐ray diffraction studies revealed that the crystals belonged to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 83.7, b = 107.2, c = 79.0 Å. A data set has been collected to 2.2 Å resolution.
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