寨卡病毒NS3解旋酶的晶体结构。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2016-05-25 DOI:10.2210/pdb5vi7/pdb

S. Nocadello, S. Light, G. Minasov, L. Shuvalova, A. CARDONA-CORREA, Isabel Ojeda, J. Vargas, Michael E. Johnson, Hyun Lee, W. Anderson

引用次数: 0

摘要

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Crystal structure of the Zika virus NS3 helicase.

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来源期刊

Acta Crystallographica Section D: Biological Crystallography 生物-晶体学

自引率

13.60%

发文量

审稿时长

3 months

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.