Charge-density analysis of an iron–sulfur protein at an ultra-high resolution of 0.48 Å
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature18001.pdf
Reference41 articles.
1. Hendrickson, W. A. Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252–270 (1985)
2. Wlodawer, A., Minor, W., Dauter, Z. & Jaskolski, M. Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination. FEBS J. 280, 5705–5736 (2013)
3. Rokob, T. A., Srnec, M. & Rulíšek, L. Theoretical calculations of physico-chemical and spectroscopic properties of bioinorganic systems: current limits and perspectives. Dalton Trans. 41, 5754–5768 (2012)
4. Nogi, T., Fathir, I., Kobayashi, M., Nozawa, T. & Miki, K. Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl Acad. Sci. USA 97, 13561–13566 (2000)
5. Liu, L., Nogi, T., Kobayashi, M., Nozawa, T. & Miki, K. Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum. Acta Crystallogr. D 58, 1085–1091 (2002)
Cited by 95 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. WhiB-like proteins: Diversity of structure, function and mechanism;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2024-10
2. CheckMyMetal (CMM): validating metal-binding sites in X-ray and cryo-EM data;IUCrJ;2024-08-14
3. On electrostatic interactions of adenosine triphosphate–insulin‐degrading enzyme revealed by quantum mechanics/molecular mechanics and molecular dynamics;Quantitative Biology;2024-08-12
4. MolDStruct: Modeling the dynamics and structure of matter exposed to ultrafast x-ray lasers with hybrid collisional-radiative/molecular dynamics;The Journal of Chemical Physics;2024-05-10
5. Gauging Iron–Sulfur Cubane Reactivity from Covalency: Trends with Oxidation State;JACS Au;2024-04-05
1.学者识别学者识别
2.学术分析学术分析
3.人才评估人才评估
"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370
www.globalauthorid.com
TOP
Copyright © 2019-2024 北京同舟云网络信息技术有限公司 京公网安备11010802033243号 京ICP备18003416号-3