EMhub:用于科学设施数据管理和即时处理的网络平台。

IF 2.6 4区 生物学 Q2 BIOCHEMICAL RESEARCH METHODS Acta Crystallographica. Section D, Structural Biology Pub Date : 2024-11-01 Epub Date: 2024-10-07 DOI:10.1107/S2059798324009471
Jose M de la Rosa-Trevin, Grigory Sharov, Stefan Fleischmann, Dustin Morado, John C Bollinger, Darcie J Miller, Daniel S Terry, Scott C Blanchard, Israel S Fernandez, Marta Carroni
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引用次数: 0

摘要

大多数科研机构都能快速生成大量异构数据。管理用户、仪器、报告和发票带来了额外的挑战。为应对这些挑战,EMhub 推出了一个网络平台,旨在支持科学设施的日常运作和记录保存。EMhub 可以轻松管理用户信息、仪器、预订和项目。该应用程序最初是为满足低温电子显微镜设施的需要而开发的,但其功能和适应性已被证明足以扩展到其他数据生成中心。EMHub 核心功能的模块化特性使其得以扩展。该应用程序允许通过 REST API 连接外部进程,自动执行文件夹创建、用户和密码生成以及实时数据处理管道执行等任务。EMhub 已在瑞典国家低温电子显微镜设施使用多年,并已安装在圣裘德儿童研究医院结构生物学部的低温电子显微镜中心。该系统采用了全自动单颗粒管道,可进行即时数据处理和分析。在圣裘德,X 射线晶体学中心和单分子成像中心已经扩展了该平台,以支持其操作和数据管理工作流程。
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EMhub: a web platform for data management and on-the-fly processing in scientific facilities.

Most scientific facilities produce large amounts of heterogeneous data at a rapid pace. Managing users, instruments, reports and invoices presents additional challenges. To address these challenges, EMhub, a web platform designed to support the daily operations and record-keeping of a scientific facility, has been introduced. EMhub enables the easy management of user information, instruments, bookings and projects. The application was initially developed to meet the needs of a cryoEM facility, but its functionality and adaptability have proven to be broad enough to be extended to other data-generating centers. The expansion of EMHub is enabled by the modular nature of its core functionalities. The application allows external processes to be connected via a REST API, automating tasks such as folder creation, user and password generation, and the execution of real-time data-processing pipelines. EMhub has been used for several years at the Swedish National CryoEM Facility and has been installed in the CryoEM center at the Structural Biology Department at St. Jude Children's Research Hospital. A fully automated single-particle pipeline has been implemented for on-the-fly data processing and analysis. At St. Jude, the X-Ray Crystallography Center and the Single-Molecule Imaging Center have already expanded the platform to support their operational and data-management workflows.

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来源期刊
Acta Crystallographica. Section D, Structural Biology
Acta Crystallographica. Section D, Structural Biology BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY
CiteScore
4.50
自引率
13.60%
发文量
216
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.
期刊最新文献
Reconsideration of the P-clusters in VFe proteins using the bond-valence method: towards their electron transfer and protonation. Making the most of an abundance of data. AlphaFold-guided molecular replacement for solving challenging crystal structures. Useful experimental aspects of small-wedge synchrotron crystallography for accurate structure analysis of protein molecules. Peter Main (1939-2024).
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