z-logo
Premium
Growth of large protein crystals by a large‐scale hanging‐drop method
Author(s) -
Kakinouchi Keisuke,
Nakamura Tsutomu,
Tamada Taro,
Adachi Hiroaki,
Sugiyama Shigeru,
Maruyama Mihoko,
Takahashi Yoshinori,
Takano Kazufumi,
Murakami Satoshi,
Inoue Tsuyoshi,
Kuroki Ryota,
Mori Yusuke,
Matsumura Hiroyoshi
Publication year - 2010
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889810015967
Subject(s) - protein crystallization , drop (telecommunication) , mosaicity , crystal (programming language) , crystallization , materials science , crystallography , capillary action , ice crystals , diffraction , crystal growth , chemistry , optics , x ray crystallography , composite material , physics , telecommunications , organic chemistry , computer science , programming language
A method for growing large protein crystals is described. In this method, a cut pipette tip is used to hang large‐scale droplets (maximum volume 200 µl) consisting of protein and precipitating agents. A crystal grows at the vapor–liquid interface; thereafter the grown crystal can be retrieved by droplet–droplet contact both for repeated macroseeding and for mounting crystals in a capillary. Crystallization experiments with peroxiredoxin of Aeropyrum pernix K1 (thioredoxin peroxidase, ApTPx) and hen egg white lysozyme demonstrated that this large‐scale hanging‐drop method could produce a large‐volume crystal very effectively. A neutron diffraction experiment confirmed that an ApTPx crystal (6.2 mm 3 ) obtained by this method diffracted to beyond 3.5 Å resolution.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom