The impact of Lys→Arg surface mutations on the crystallization of the globular domain of RhoGDI-Reference-Cited by-同舟云学术

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The impact of Lys→Arg surface mutations on the crystallization of the globular domain of RhoGDI

Published:2004-01-24 Issue:2 Volume:60 Page:275-280
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Czepas Jan,Devedjiev Yancho,Krowarsch Daniel,Derewenda Urszula,Otlewski Jacek,Derewenda Zygmunt S.

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2004/02/00/ea5008/ea5008.pdf

Cited by 47 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Antigen‐binding fragments with improved crystal lattice packing and enhanced conformational flexibility at the elbow region as crystallization chaperones;Protein Science;2024-06-26

2. Systematic enhancement of protein crystallization efficiency by bulk lysine‐to‐arginine (KR) substitution;Protein Science;2024-02-15

3. Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution;2023-06-06

4. Nonspecific Binding of Adenosine Tripolyphosphate and Tripolyphosphate Modulates the Phase Behavior of Lysozyme;Journal of the American Chemical Society;2023-01-06

5. Structural Basis for Reduced Dynamics of Three Engineered HNH Endonuclease Lys-to-Ala Mutants for the Clustered Regularly Interspaced Short Palindromic Repeat (CRISPR)-Associated 9 (CRISPR/Cas9) Enzyme;Biochemistry;2022-04-14

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