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2024-03-07 18:30:18

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为什么E＝mC2 - 知乎

为什么E＝mC2 - 知乎切换模式写文章登录/注册为什么E＝mC2GCGA管理学1934年，爱因斯坦在黑板上推导狭义相对论。爱因斯坦最著名的方程式E=mc²，是科学史上最广为人知的一个公式，尽管并不是所有人都深知其含义。该公式表示一个物体的能量等于物体的质量乘以光速的平方。根据狭义相对论，质量和能量是等价的，并且是同一个物体的两种不同表现。物质都具有质量：大到星系、恒星和行星，小到分子、原子和基本粒子。不管它们有多小，所有我们已知的物质都有基本的性质：质量。也就是说即使它不再运动，或者让它慢慢减速直至完全的静止，它仍然会影响着宇宙中其它的物体。每个单独的质量对宇宙中其它的物体都具有引力作用，不管距离多远。它试图吸引所有其它的物体，但也经历着被所有其它的物体所吸引。此外，它的存在也具有一定的能量。描述了大质量物体（比如太阳和地球）是如何影响时空的构造。但是，这并不意味着只有具有质量的物体才能具备能量。在宇宙中也有完全没有质量的粒子，比如光子。光子也携带一定量的能量，它们可以与其它的物体作用，并被吸收，以及传递能量给其它的物体。足够能量的光可以加热物体，并传递额外的动能（和速度）给它们。光子会把原子中的电子踢到更高的能量等级，或者完全电离它们，这都取决于光子的能量。此外，无质量粒子（比如光子）的能量只由它们的频率和波长决定，两者的乘积等于无质量粒子的速度，即光速。波长越长，频率越小，能量也越低。反之短波长意味着拥有更高的频率和能量。波长越长的光子能量越小。但是所有的光子，不论其波长和能量为何，它们的速度都一样，即光速。在物理上，我们把能量当做完成某项任务的能力，我们称之为做功的能力。那么有质量粒子和无质量粒子之间的能量有什么关联？我们可以想象，将一个电子（物质）和一个正电子（反物质）相互碰撞，它们会湮灭并产生无质量粒子（比如两个光子）。但是为什么两个光子的能量等于电子（和正电子）的质量乘以光速的平方？为什么是E=mc²，而不是E=2mc²，或者是其它常数（¼ 或 π 等）？爱因斯坦在讲堂上推导狭义相对论 @1934年。有趣的是，如果狭义相对论是正确的，那么方程式必须是E=mc²。为什么是会这样？要回答这个问题，我们先开始想象在你空间中有一个完全静止的盒子，在盒子的两边分别有两面镜子，有一个光子在盒子里朝着一端的镜子传播。如下图：思想实验的装置：一个具备动量和能量的光子在一个带有质量M的静止的（动量=0，动能=0）盒子里运动。（© E.Siegel）最初，这个盒子完全的静止，但是由于光子携带能量（和动量），当光子撞上盒子一端的镜子时就会反弹，盒子则开始向光子最初的传播方向移动。光子朝另一端的镜子再次反弹折回，使盒子的动量再次改变为零。光子将不断的来回反弹，因此盒子一半的时间向前移动，一半的时间保持静止。换句话，平均上这个盒子是在移动的，由于盒子拥有质量，它就具有一定的动能，这一切都是因为光子的能量。但更重要的是动量（是描述一个物体运动的量）这个概念。光子具有动量，其关系很简单明了：波长越短、能量越高，因此动量也越大。光子的能量取决于波长：波长越大能量越小，波长越短能量越大。为了更好的理解，我们来做一个思想实验。我需要你想象，最初当光子自身在运动时会发生什么。它具有一定的能量以及一定的动量，这两者都必须是守恒的。现在光子的能量由它的波长决定，盒子的能量由静止质量决定。此外光子具有整个系统的动量，也就是盒子的动量为零。现在光子撞上盒子，并暂时被吸收。动量和能量两者都必须守恒，它们是宇宙中最基本的守恒定律。如果光子被吸收，这意味着只有一个方法能保持动量守恒：盒子获得了一定的速度往光子移动的方向移动。吸收了光子后盒子的能量（KE）和动量（M'v）。如果盒子没有在该作用中获得了额外质量，能量和动量就不可能守恒。（© E.Siegel）现在，我们可以问自己，盒子的能量是多少？结果是我们熟知的动能公式：KE = ½mv²，m是盒子的质量，v是盒子的速度。但是，当我们比较现在盒子的能量与光子被吸收之前的能量，我们发现盒子现在的能量不够。难道是已知的物理定律在哪里错了？并不是，有一个非常简单的解决方法。盒子/光子系统的能量是盒子的静止能量加上盒子的动能再加上光子的能量。当盒子吸收光子时，大部分光子的能量转换成了盒子的质量。一旦盒子吸收光子，它的质量跟它与光子作用之前不同（增加了）。当盒子重新辐射出光子时，能量和动量仍然必须守恒。（© E.Siegel）当盒子重新辐射出光子（往相反的方向）时，它获得了更多的动量和速度（为了平衡往反方向运动具有负动量的光子），甚至更多的动能，但是它必须失去一定的静止质量来补偿。在一点点的数学计算（文末阅读原文提供了相关背景的链接），你就会发现为了得到能量守恒和动量守恒，我们最终会得到质能关系E=mc²。如果在方程式加上其它常数，就得不到守恒，每次吸收或辐射光子的时候都会得到会失去能量。直到1930年，当反物质最终被发现的时候，物理学家得到了E=mc²的第一次验证，在这之前是上述的思想实验帮助我们得到的该结果。能量守恒与动量守恒是我们现在生活在这个宇宙所要求的，这也正是为什么E=mc²。发布于 2016-07-19 09:17赞同 368 条评论分享喜欢收藏申请

emc（EMC公司）_百度百科

EMC公司）_百度百科网页新闻贴吧知道网盘图片视频地图文库资讯采购百科百度首页登录注册进入词条全站搜索帮助首页秒懂百科特色百科知识专题加入百科百科团队权威合作下载百科APP个人中心emc是一个多义词，请在下列义项上选择浏览（共13个义项）添加义项收藏查看我的收藏0有用+10emc播报讨论上传视频EMC公司EMC（易安信）为一家美国信息存储资讯科技公司，主要业务为信息存储及管理产品、服务和解决方案。EMC公司创建于1979年，总部在马萨诸塞州霍普金顿市。2003年，EMC收购了VMware。2015年10月，EMC被DELL收购。EMC公司的股票符号是EMC，在纽约股票交易所交易，并且是S&P 500成份股之一。EMC作为全球领导厂商，帮助企业和服务提供商实现运营转型，交付IT即服务。这一转型的基础是云计算。EMC通过创新的产品和服务，加速云计算之旅，帮助IT部门以更灵活、更可信和成本效益更高的方式，存储、管理、保护和分析他们的最宝贵的资产——信息。2015年10月12日，戴尔与数据存储公司EMC的并购宣布完成，最终戴尔以670亿美元收购了EMC。 [1]2016年8月31日，戴尔公司(Dell Inc.)周二表示，已取得中国监管机构的批准，计划于9月7日完成收购EMC Corp. (EMC)的交易 [2]。中文名易安信外文名EMC所处国家美国属性信息存储资讯科技公司官网http://www.emc.com/目录1发展历程2被收购后影响3公司分布4公司规模5主要产品发展历程播报编辑EMC 于1979年由1961年毕业于美国东北大学的Richard Egan [10] [14]和Roger Marino [11-13]成立在美国麻州Hopkinton市，1989年开始进入企业数据储存市场。二十多年来，EMC全心投注在各项新的储存技术，已获得了1,300个已通过或审核中的储存技术专利。无论是全球外接RAID储存系统、网络储存亦或是储存管理软件等储存专业领域，EMC均是业界公认的领导厂商。EMC 在全球超过50个国家有100个以上的分公司及经销伙伴，拥有全球最大且最专业的储存销售与服务之团队，带给客户最迅速的响应服务，客户服务满意度高达96.7%。EMC 于1988年进入亚太地区，在12个国家设有分公司或办事处；1999年在台湾设立分公司，客户群涵盖金融、电信、制造与政府等各领域。美国存储设备及软件开发商EMC共同创始人理查德·埃根（Richard Egan）于2009年8月28日在波士顿家里去世，享年73岁。他曾担任过美国驻爱尔兰大使。在埃根领导下，EMC于1986年成为上市公司。1998年，埃根当选EMC董事长。在1992年之前，埃根还曾担任过该公司总裁及CEO等职位。如今，EMC已经成为在全球拥有约4万员工的科技巨头。创建于1979 年，总部在马萨诸塞州霍普金顿市的EMC 公司（NYSE：EMC），是全球第六大企业软件公司，全球信息基础架构技术与解决方案的领先开发商与提供商，致力于帮助我们的客户加速迈上私有云之旅。在信息存储领域，多年来EMC继续保持着全球第一的领先优势。作为美国财富五百强之一，2009年全球研发投入高达14亿美元，EMC公司在全世界拥有超过四万二千名员工，在全球60个国家或地区拥有分支机构。EMC中国研发中心于2006年11月2日正式落成，分别位于上海和北京，主要负责EMC的核心软件与硬件的开发工作。其主要目标是向EMC业务部门提供先进的软件与硬件开发和质量保证功能，为中国、亚太地区和全球的客户提供世界一流的产品和服务。同时，EMC在北京也建立了基础研究实验室，从事着EMC全球领先科技包括云计算及虚拟化技术的基础研究工作。2009年7月，EMC中国研发中心正式升级为EMC中国卓越研发集团，下设存储技术研发基地、云计算研发基地、信息管理研发基地、中国实验室、全球解决方案中心和全球客户技术支持中心六大职能部门。EMC在北京、上海、广州、成都、南京、西安、武汉、沈阳、福州、乌鲁木齐、济南、杭州、昆明、重庆、青岛，郑州设立了共16家分公司。并在北京、上海、广州、成都、深圳、香港和台湾七地建立了解决方案中心。为了帮助用户更好地掌握和利用EMC产品和服务，EMC在全国各地设立了35家服务中心，并于2004年开通了全球支持中心中文服务热线。EMC还在香港建立配送中心，加快市场响应速度，提高客户满意度。2015年6月19日，EMC在对其XtremIO和ScaleIO系统推出了软件插件，利用简易的Docker存储容器实现共享存储。 [3]Dell将以每股33.15美元收购EMC，包含现金和特殊股票，其中现金部分占每股24.05美元。交易总额达近670亿美元，是科技史上最大并购。VMware维持独立公开上市。根据协议，EMC公司股东将获得每股24.05美元现金，加EMC在VMware业务部分经济利益的追踪股票。根据交易结束时EMC流通股票的估计数字，EMC股东预期从每股EMC股票收到约0.111股新的追踪股票。举例来说，假设2015年10月7日星期三，VMware盘中成交量加权平均的每股追踪股票估值为81.78美元，EMC股东将收到每股33.15美元的综合价值，交易的总价值将约为670亿美元。由于两支股票不同的特性和权益，跟踪股票的价值可能会随着VMware股票的价格而变化。 [4]被收购后影响播报编辑EMC用户担心戴尔的收购451 Research LLC的分析师Dan Harrington、Michelle Bailey以及Simon Robinson表示在戴尔、EMC合并一事中用户的处境被忽略了，各方只关注了金融数字方面的元素。根据451 Research调查显示，有40%的EMC用户对收购持悲观态度，在戴尔这面有15%。受访的447名企业购买者中，有1/4的用户对戴尔收购后是否依然购买产生犹豫。451分析师分析这将给更多厂商带来机会，原先选用EMC的用户可能会考虑其他厂商的方案。调查显示，39%的受访者认为两家公司都会从本次收购中获益，不过27%的受访者担心这会分散两家公司。戴尔需要极力获取EMC用户的信任，毕竟之前他们将戴尔视作低端PC供应商。如果戴尔能给新的客户群提供一个明确的产品路线图，可能会有所缓解。对网络专业人员来说，路线图同样重要，是对VMware未来建立信任的关键所在。 [5]公司分布播报编辑地区地址邮编美国（总部）EMC Corporation 176 South Street Hopkinton , MA 01748 United States01748中国北京15/F, Hyundai Motor Tower No. 38 Xiaoyun Road Chaoyang District Beijing100027中国上海23 and 24 F, Xinmei Union Square No. 999 Pudong South Road Shanghai200120中国广州Unit 7401, Level 74, CITIC Plaza, 233 Bei Road Tianhe District Guangzhou510613中国南京1752-1753, World Trade Center No. 2 Han Zhong Lu Nanjing210005公司规模播报编辑排名公司财富500强排名2007年净利润增幅1微软44141亿美元12%2IBM15104亿美元10%3思科7173亿美元31%4惠普1473亿美元17%5英特尔6070亿美元38%6甲骨文13743亿美元26%7谷歌15042亿美元37%8苹果10335亿美元76%9高通29733亿美元34%10戴尔3429亿美元14%11德州仪器18527亿美元39%12康宁41722亿美元90%13应用材料27017亿美元13%14EMC20117亿美元36%EMC在全球拥有53500多名员工，在全球85个国家有400多个办事处和众多合作伙伴。我们拥有世界上最大的销售和服务力量，主要从事信息基础架构工作，我们与全球的技术、外包、系统集成、服务和分销合作伙伴网络紧密合作。EMC（纽约证交所代码：EMC）是一家在纽约证券交易所上市的公司，是标准普尔500指数中的一个组成部分。2011年，EMC入选北美道琼斯可持续发展指数（DJSI），其目的是在全球范围内跟踪以可持续发展为主导的领先公司的财务业绩。我们致力于以对社会和环境负责任的方式行事，在当地社区和全球社区中扮演细心周到邻居的角色。我们在区域性最佳工作地的评比当中获得的分数较高。2010年，EMC财年综合收入达到创纪录的170亿美元。EMC在纽约股票交易所交易，是标准普尔指数的成份股之一。2011年，EMC名列美国《财富》计算机行业最受尊敬公司第二位、美国《财富》500强企业152位。合并EMC后，戴尔将摇身一变，由一个主要为中小企业提供服务的IT商瞬间变成能够服务大型企业的厂商，有分析师说道。从戴尔网络组合产品角度来看，戴尔将会将其服务器、网络与EMC的存储结合在一起，面向数据中心销售超融合系统。这些系统很可能通过VMware、思科和EMC的VCE联合进行出售。三家厂商在2009年建立合作销售虚拟化、网络和存储，并打包为企业建设私有云。 [6]主要产品播报编辑EMC的主要产品为企业级服务器存储硬件和软件，以及与存储相关的网络产品。主要有以下的产品：高端存储EMC高端存储主要为Symmetrix系列和VNX系列，Symmetrix系列主要有VMAX ，VMAXe,DMX-4，DMX-3。VNX系列主要有VNX和VNXe两种产品，具体型号有VNX5100,VNX5300,VNX5500,VNX5700和VNX7500.中端存储EMC中端存储主要为CLARiiON系列，主要有CX3、CX4和AX4等型号。NAS存储NAS存储主要有NS120，NS480，NS960等型号。云备份企业级云备份系统主要有Mozy等产品。Virtustream2015年10月，EMC公司和VMware宣布，通过结合其各自的云能力，以及现有的Virtustream云产品，计划打造EMC联邦全新的云服务业务，新业务将在Virtustream品牌下运营。Virtustream将由VMware和EMC联合拥有，由Virtustream首席执行官Rodney Rogers领导。双方正在敲定交易的最终协议。从2016年第一季度开始，Virtustream的财务业绩将整合至VMware的财务报表中。网络拓补图Virtustream将集成这些资产，为客户提供统一的基础设施即服务产品，旨在通过一个包含全方位服务和部署选项的产品组合，支持完整的业务工作负载。该业务将集成现有的本地EMC联邦私有云部署，并将其扩展至公共云中，让开发者、管理者、架构师和终端用户保持共同的使用体验。Virtustream的云服务将通过合作伙伴直接交付给客户。 [7]XtremIO在2013年11月，EMC就已经正式发布了one-brick、two-brick和four-brick配置的XtremIO X-Brick阵列。每个brick包含10TB或20TB的闪存空间。而新的Starter X-Brick包含有5TB或是10TB闪存空间。考虑最大容量的情形，新的six-X-Brick集群拥有12个活跃的控制器，通过冗余磁盘阵列技术的使用，能够带来90TB的初始容量。EMC在2014年7月扩展了它的XtremIO全闪存阵列平台，新增了入门级配置Starter X-Brick，规模可达到6个节点，同时还有线内压缩、静态数据加密和可写快照技术的集成 [8]。DSSD D5DSSD D5可以提供高达10,000,000的IOPS，延迟仅为100微秒，带宽则可以达到每秒100GB，5机柜配置的裸存储空间则为144TB。该系统可以被最多48个直连客户端进行冗余访问。它采用了dual-ported PCIe Gen 3以及NVMe服务器闪存技术。EMC在搭建D5闪存模块时还采用了裸NAND颗粒。每台D5包括36个闪存模块，可用空间为36TB、72TB或者144TB。在可靠性和可用性方面则提供了DSSD专有的Cubic RAID、动态损耗均衡、闪存物理控制以及系统闲时垃圾回收等技术。 [9]新手上路成长任务编辑入门编辑规则本人编辑我有疑问内容质疑在线客服官方贴吧意见反馈投诉建议举报不良信息未通过词条申诉投诉侵权信息封禁查询与解封©2024 Baidu 使用百度前必读 | 百科协议 | 隐私政策 | 百度百科合作平台 | 京ICP证030173号京公网安备110000020000

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E = mc² | Equation, Explanation, & Proof | Britannica

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ER 膜蛋白复合亚基 2（EMC2）基因 | MCE

— Master of Bioactive Molecules

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E = mc² Calculator

We’re hiring!EmbedShare viaE = mc² CalculatorCreated by Bogna SzykReviewed by Steven WoodingLast updated: Jan 18, 2024Table of contents:Einstein's theory of relativityMass energy equivalence formulaConsequences of E = mc²FAQYou can bet that anyone you meet will at least have heard about this famous equation. You have probably come across it a hundred times yourself. But what does E equals mc squared actually mean? What is the mysterious mass-energy equivalence principle? What had Einstein to do with it? Continue reading to find out!Einstein's theory of relativity

In 1905, Albert Einstein proposed a theory that stated that mass and energy are equivalent. It meant that the law of conservation of energy (it says that the sum of potential energy and kinetic energy of a body is constant) and the law of conservation of mass are, in fact, the same. Also, Einstein stated that even a particle at rest has some energy, called its rest energy. You can find more information about the energy of an object in our potential energy calculator and our kinetic energy calculator.Mass energy equivalence formula

All right, you probably know that:E=mc2E = mc^2E=mc2But what exactly do the letters in this famous equation stand for?

mmm – Mass of an object in kilograms (kg);

ccc – Speed of light – a constant value of 299,792,458 m/s; and

EEE – Rest energy of the object in joules (J).

Make sure that the mass of the object is in the unit of kilograms. If not, you can use our weight converter to express the object's mass value in kilograms easily. You can visit our energy conversion calculator if you want to learn how to convert the calculated energy value into other units of energy.Consequences of E = mc²

Once you start to think about it, the consequences of the formulation of E = mc² equation were astounding. Einstein proposed a world in which mass is just energy waiting to be 'set free'. And not just some energy – an enormous amount of it.

The average adult weight is 62 kg. Such a person, according to Einstein, has a rest energy of 5.6 × 1012 megajoules (MJ). You can check it with our E = mc² calculator. Just for comparison, the bomb dropped on Nagasaki had the energy of 8.4 × 107 MJ. In essence, if you managed to explode and set all of your rest energy free (which is not achievable... yet), you would cause the same destruction as over 66,000 nuclear bombs. Saying it's a lot is definitely an understatement.

This formula was a lifesaver for everyone trying to understand how the universe works. It explained why radioactive materials don't 'melt' while emitting streams of particles (it is because of the extreme efficiency of converting mass to energy). It also explains why the stars don't run out of hydrogen, their primary fuel, for billions of years. Suddenly, the age of the universe appeared much more credible. To learn more about this topic, you can also explore our relativistic kinetic energy calculator, where the formula is almost identical.FAQ

What is c in E=mc²?c denotes the speed of light in vacuum (299,792,458 m/s). That means that even a tiny mass is equivalent to a significant amount of rest energy.What is the meaning of E=mc²?Mass and energy are interchangeable. On the one hand, we can turn mass into energy as in nuclear power plants. On the other hand, high-energy photons can create matter (usually as the particle-antiparticle pair, e.g., electron and positron).How much energy does a Uranium-235 fission reaction yields?Assuming that 0.1% of the total mass of Uranium-235 converts to energy through fission reaction:

Take the 235U mass, which is about 235 u.

Convert the mass to kilograms: m = 235 × 1.66×10⁻²⁷ kg = 3.9×10⁻²⁵ kg.

Evalue the mass that converts to energy: Δm = 0.1% × 3.9·10⁻²⁵ kg = 3.9×10⁻²⁸ kg.

Multiply it by the squared speed of light, c² = 9×10¹⁶ m²/s².

The resulting energy equals about 3.51×10⁻¹¹ J or 219 MeV.

What is the mass deficit for the D-T fusion reaction?The deuterium-tritium fusion reaction yields 17.6 MeV energy. To find the mass deficit:

Convert the energy to joules: 17.6 MeV = 2.82×10⁻¹² J.

Divide it by the squared speed of light: 2.82×10⁻¹² / 9×10¹⁶ = 3.13×10⁻²⁹ kg.

We can also write it using the atomic unis: 3.13×10⁻²⁹ / 1.66×10⁻²⁷ = 0.019 u.

Bogna SzykMasslbEnergyMJCheck out 8 similar relativity calculators Bug-rivet paradoxElectron speedGravitational time dilation… 5 morePeople also viewed…Black FridayHow to get best deals on Black Friday? The struggle is real, let us help you with this Black Friday calculator!Black Friday CalculatorIdeal egg boilingQuantum physicist's take on boiling the perfect egg. Includes times for quarter and half-boiled eggs.Ideal Egg Boiling CalculatorPressureUse the pressure calculator to find the pressure exerted by a force on a specific area.Pressure CalculatorSpecific impulseEstimate how efficiently an engine generates thrust using the specific impulse calculator.Specific Impulse CalculatorOther Physics calculatorsEnglishEnglishPortuguese (Português)About Omni CalculatorCalculator collectionsEditorial policiesAll calculatorsPress kitBlogJournalist's Guide to NumbersContactPartnershipsWe’re hiring!Copyright by Omni Calculator sp. z o.o.Privacy, Cookies & Terms of ServiceBiology (98)Chemistry (98)Construction (144)Conversion (292)Ecology (30)Everyday life (261)Finance (565)Food (66)Health (439)Math (660)Physics (508)Sports (104)Statistics (182)Other (180)Discover Omni (40)

Structure of the ER membrane complex, a transmembrane-domain insertase | Nature

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Published: 03 June 2020

Structure of the ER membrane complex, a transmembrane-domain insertase

Lin Bai

ORCID: orcid.org/0000-0002-7535-78191, Qinglong You1, Xiang Feng1, Amanda Kovach1 & …Huilin Li

ORCID: orcid.org/0000-0001-8085-89281 Show authors

Nature

volume 584, pages 475–478 (2020)Cite this article

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Cryoelectron microscopyEnzyme mechanismsProtein translocation

AbstractThe endoplasmic reticulum (ER) membrane complex (EMC) cooperates with the Sec61 translocon to co-translationally insert a transmembrane helix (TMH) of many multi-pass integral membrane proteins into the ER membrane, and it is also responsible for inserting the TMH of some tail-anchored proteins1,2,3. How EMC accomplishes this feat has been unclear. Here we report the first, to our knowledge, cryo-electron microscopy structure of the eukaryotic EMC. We found that the Saccharomyces cerevisiae EMC contains eight subunits (Emc1–6, Emc7 and Emc10), has a large lumenal region and a smaller cytosolic region, and has a transmembrane region formed by Emc4, Emc5 and Emc6 plus the transmembrane domains of Emc1 and Emc3. We identified a five-TMH fold centred around Emc3 that resembles the prokaryotic YidC insertase and that delineates a largely hydrophilic client protein pocket. The transmembrane domain of Emc4 tilts away from the main transmembrane region of EMC and is partially mobile. Mutational studies demonstrated that the flexibility of Emc4 and the hydrophilicity of the client pocket are required for EMC function. The EMC structure reveals notable evolutionary conservation with the prokaryotic insertases4,5, suggests that eukaryotic TMH insertion involves a similar mechanism, and provides a framework for detailed understanding of membrane insertion for numerous eukaryotic integral membrane proteins and tail-anchored proteins.

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Fig. 1: Purification of the yeast EMC and identification of EMC client proteins.Fig. 2: Structure of the yeast EMC.Fig. 3: The transmembrane region of the yeast EMC contains a client-binding pocket.Fig. 4: A model for client TMH insertion by the eukaryotic EMC.

Data availability

The cryo-EM 3D map of the S. cerevisiae EMC complex has been deposited at the Electron Microscopy Data Bank (EMDB) database with accession code EMD-21587. The corresponding atomic model was deposited at the RCSB Protein Data Bank (PDB) with accession code 6WB9. The TMT mass spectrometry data and the real-space correlation coefficients of all residues with experimental densities data are provided in Supplementary Tables 1–3. The uncropped SDS–PAGE gels used in Figs. 1a, 3g and Extended Data Fig. 6b can be found in Supplementary Fig. 1.

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Download referencesAcknowledgementsCryo-EM images were collected in the David Van Andel Advanced Cryo-Electron Microscopy Suite at Van Andel Research Institute. We thank G. Zhao and X. Meng for assistance with data collection and D. Nadziejka for critical reading of the manuscript. This work was supported by the US National Institutes of Health (NIH) (R01 CA231466 to H.L.) and Van Andel Institute (to H.L.).Author informationAuthors and AffiliationsStructural Biology Program, Van Andel Institute, Grand Rapids, MI, USALin Bai, Qinglong You, Xiang Feng, Amanda Kovach & Huilin LiAuthorsLin BaiView author publicationsYou can also search for this author in

PubMed Google ScholarQinglong YouView author publicationsYou can also search for this author in

PubMed Google ScholarXiang FengView author publicationsYou can also search for this author in

PubMed Google ScholarAmanda KovachView author publicationsYou can also search for this author in

PubMed Google ScholarHuilin LiView author publicationsYou can also search for this author in

PubMed Google ScholarContributionsL.B. and H.L. conceived and designed experiments. L.B. performed most of the experiments. Q.Y., X.F. and A.K. helped with sample preparation and functional assays. L.B. and H.L. analysed the data and wrote the manuscript.Corresponding authorsCorrespondence to

Lin Bai or Huilin Li.Ethics declarations

Competing interests

The authors declare no competing interests.

Additional informationPeer review information Nature thanks Friedrich Förster and the other, anonymous, reviewer(s) for their contribution to the peer review of this work.Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.Extended data figures and tablesExtended Data Fig. 1 Data processing and validation of cryo-EM micrographs and 3D reconstruction.a, Gel filtration profile of the EMC complex. This experiment was repeated more than five times with similar results. b, c, Representative electron micrograph and selected reference-free 2D class averages of the EMC. A total of 4,260 micrographs were recorded with similar quality. d, Cryo-EM data-processing procedure. e, Gold-standard Fourier shell correlations of two independent half maps with or without mask, and with randomized phases, and the validation correlation curves of the atomic model by comparing the model with the final map or with the two half maps. f, Local-resolution map of the 3D map. g, Angular distribution of particles used in the final reconstruction of the 3D map.Extended Data Fig. 2 Protein abundance and localization of nine putative EMC clients in wild-type and Emc3-knockout yeast strains.The eGFP is appended to the C termini of the genes. Scale bar, 10 μm. This experiment was repeated three times with similar results.Extended Data Fig. 3 Cryo-EM 3D density map of the EMC.a–d, The surface-rendered map is shown in front view (a), left side view (b), right side view (c), back view (d), bottom (lumenal) view (e), and top (cytosolic) view (f). Maps are coloured by individual subunits.Extended Data Fig. 4 The fitting of the atomic model and the 3D map in selected regions.3D density map and atomic model of selected regions in each of the eight EMC subunits, as well as the densities of atomic models of the two phospholipid molecules. C-ter, C-terminal domain; HH, horizontal helix; N-ter, N-terminal domain.Extended Data Fig. 5 Structure of the lumenal and cytosolic regions of the yeast EMC.a, Structure of the EMC lumenal region shown in front side and bottom (lumenal) views. The interface area between the C-terminal loop of Emc4 and the NTD2 of Emc1 is outlined by a red rectangle. The dotted black area marks the NTD2 of Emc1, which is an eight-bladed β-propeller. b, Superposition of the NTD2 β-propeller of Emc1 with the structure of a fungus chaperone protein Sqt1 (PDB code 4ZN4). c, Enlarged view of the red-outlined region in a. d, Structure of the EMC cytosolic region in top (cytosolic) and front side views. Emc2 as the organizing centre is shown in cartoon, and the cytosolic domains of Emc3, Emc4 and Emc5 are shown as cylinders.Extended Data Fig. 6 In vitro binding assays between the purified EMC and the TOM complex.a, Gel filtration profiles of the EMC alone, the TOM complex alone, and the mixture of the EMC–TOM complexes. No peak corresponding to the assembly of the EMC–TOM complex was observed. The experiment was repeated three times yielding similar results. b, Peak fractions of the EMC–TOM mixture in a were checked by the Coomassie blue-stained SDS–PAGE gel. The band densities suggest that the peak is simply an overlap of the unbound and separate EMC and TOM. For gel source data, see Supplementary Fig. 1.Extended Data Fig. 7 The 3D EM map of the EMC surface rendered at a low display threshold.The bound lipids/detergents surrounding the transmembrane region of the EMC complex are visible in this low-threshold display. The atomic model in cartoon is superimposed on the 3D map. Note that the horizontal helix of Emc1 is at the ER lumen–membrane boundary.Extended Data Fig. 8 Structural comparison between yeast EMC and E. coli YidC.a, Structure of EMC in cartoon. b, Structure of E. coli YidC in cartoon (PDB code 3WVF). c, Superposed structures of EMC (colour) and YidC (dark grey).Extended Data Fig. 9 Comparisons of protein abundance, localization, and growth of the mutant yeast strains with the wild-type cells.a, Protein abundance and localization of two putative EMC clients (Mrh1 and Fet3) in wild-type and EMC3(K26L) mutant yeast strains. The eGFP is appended to the C termini of the genes. b, Growth experiments of yeast strains containing Emc4 linker loop truncations. The three truncations were Emc4(∆56–60), Emc4(∆51–60), and Emc4(∆46–60). Experiments in a and b were repeated three times with similar results.Extended Data Table 1 Cryo-EM data collection, refinement, and validation statisticsCryo-EM data collection, refinement, and validation statisticsFull size tableSupplementary informationSupplementary Figure 1Uncropped SDS-PAGE gels used for preparing Fig. 1a, Fig. 3g, and Extended Data Fig. 6b.Reporting SummarySupplementary Table 1 | EMC dependent proteins identified by TMT mass spectrometryThe N positions were either from literature as cited or as predicted by TMHMM Server V. 2.0.Supplementary Table 2 | TMT mass spectrometry results of WT and EMC knockout cellsSupplementary Table 3 | The list of real-space correlation coefficients of all residues with experimental densitiesThe correlations were calculated for each amino acid between the atomic model and the 3D density map by PHENIX-MolProbity.Supplementary Video 1 | Cryo-EM structure of the EMC complexA surface rendering of the 3D map, superimposed with the atomic model, is shown rotating around a vertical axis by 360°, followed by another 360° rotation around a horizontal axis. The eight subunits are individually colored. The red densities are from the five resolved N-glycans.Rights and permissionsReprints and permissionsAbout this articleCite this articleBai, L., You, Q., Feng, X. et al. Structure of the ER membrane complex, a transmembrane-domain insertase.

Nature 584, 475–478 (2020). https://doi.org/10.1038/s41586-020-2389-3Download citationReceived: 04 February 2019Accepted: 07 April 2020Published: 03 June 2020Issue Date: 20 August 2020DOI: https://doi.org/10.1038/s41586-020-2389-3Share this articleAnyone you share the following link with will be able to read this content:Get shareable linkSorry, a shareable link is not currently available for this article.Copy to clipboard

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Molecular simulation is one of the most dynamic areas of scientific computing. Its field of application is very broad, ranging from theoretical chemistry and drug design to materials science and nanotechnology. Its importance in modern science has been acknowledged by two Nobel Prizes (Kohn & Pople in 1998; Karplus, Levitt & Warshel in 2013). It is also a gold mine of exciting problems for mathematicians and computer scientists.

EMC2 is an ERC Synergy project that aims to overcome some of the current limitations in the field of molecular simulation and aims to provide academic communities and industrial companies with new generation, dramatically faster and quantitatively reliable molecular simulation software. This will enable those communities to address major technological and societal challenges of the 21st century in health, energy and the environment for instance.

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Oct 31, 2023(organized by GDR NBODY with support from CNRS INC, LCT, LJLL, and ERC EMC2) Date: 5-7 June 2023 Location: Sorbonne Université, Pierre et Marie Curie (or Jussieu) campus, 4 place Jussieu, 75005, Paris. Laboratoire Jacques-Louis Lions, tower/corridor 15-16, 3rd floor,...

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The European Research Council offers many grants to support researchers, the Synergy Grants enable two to four Principal Investigators (PIs) and their teams to bring together complementary skills, knowledge, and resources in new ways, in order to address jointly ambitious research questions. Selected projects receive funds for six years and aim to cross the boundaries between different fields of research, with an emphasis on the synergetic effect of scientific excellence.

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The “Extreme-scale Mathematically-based Computational Chemistry” project aims to achieve scientific breakthroughs in this field by gathering the expertise of a multidisciplinary community at the interfaces of four disciplines: mathematics, chemistry, physics and computer science.

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