Solution-stirring method improves crystal quality of human triosephosphate isomerase-Reference-Cited by-同舟云学术

Solution-stirring method improves crystal quality of human triosephosphate isomerase

Published:2006-01 Issue:1 Volume:101 Page:83-86
ISSN:1389-1723
Container-title:Journal of Bioscience and Bioengineering
language:en
Short-container-title:Journal of Bioscience and Bioengineering

Author:

Adachi Hiroaki,Niino Ai,Kinoshita Takayoshi,Warizaya Masaichi,Maruki Riyo,Takano Kazufumi,Matsumura Hiroyoshi,Inoue Tsuyoshi,Murakami Satoshi,Mori Yusuke,Sasaki Takatomo

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Reference15 articles.

1. Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design;Velanker;Structure,1997

2. Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme;Mande;Protein Sci.,1994

3. Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method;Kinoshita;Acta Crystallogr.,2005

4. Improving the quality of protein crystals using a stirring crystallization;Adachi;Jpn. J. Appl. Phys.,2004

5. Control of protein crystal nucleation and growth using stirring solution;Niino;Jpn. J. Appl. Phys.,2004

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