{"id":5353,"date":"2015-09-22T18:58:23","date_gmt":"2015-09-22T16:58:23","guid":{"rendered":"http:\/\/news.embl.de\/?p=5353"},"modified":"2025-07-14T13:17:25","modified_gmt":"2025-07-14T11:17:25","slug":"1509-massif1","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/1509-massif1\/","title":{"rendered":"MASSIFly efficient"},"content":{"rendered":"\n

MASSIF-1<\/a>, the first beamline of the Massively Automated Sample Selection Integrated Facility, is jointly operated by ESRF and EMBL, in Grenoble. This ground-breaking tool provides European structural biologists with a fully automated service for sample evaluation and data collection from crystals of macromolecules. Scientists feed their experimental requirements into the beamline software while their samples enter a queuing system. The crystals are then located and screened automatically, and the data acquired without any human intervention.<\/p>\n\n\n\n

\u201cThe world-leading automation developed on MASSIF-1 means that as much data as possible is extracted from every sample and the robot never gets tired,\u201d explains Matthew Bowler, MASSIF-1 beamline scientist at EMBL Grenoble.<\/p>\n\n\n\n

This system both frees up the time of the scientists \u2013 who can focus better on analyzing the collected data \u2013 and improves the quality and the quantity of information collected. The automatic routine is better at locating the crystals and choosing the right angle for the beam than the human eye. In addition, more crystals can be efficiently screened: this aspect was crucial for the 10,000th crystal, the NtrX protein from Brucella abortus<\/em>.<\/p>\n\n\n\n

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The world-leading automation developed on MASSIF-1 means that as much data as possible is extracted from every sample and the robot never gets tired<\/p>\n<\/blockquote>\n\n\n\n

NtrX is made of 3 well-characterised domains, but their 3D arrangement has never been described. To tackle this question Ignacio Fernandez, PhD student from the Fundacion Instituto Leloir, Buenos Aires, Argentina, visiting EMBL Grenoble as one of six young Argentinean scientists supported by the Argentinian Ministry of Science, Technology and Productive Innovation, and Irina Cornaciu, a postdoctoral fellow at EMBL Grenoble, produced and crystalised the protein in different states: active, inactive, with its target nucleotide attached, without its target nucleotide\u2026 In total they screened through 10,000 different conditions to generate over 100 crystals.<\/p>\n\n\n\n

\u201cTo my knowledge, MASSIF-1 is the only beamline that can cope with the volume of crystals we generated, and screen them rapidly,\u201d explains Josan M\u00e1rquez<\/a> group leader at EMBL Grenoble. \u201cIt was crucial to the success of this project.\u201d More generally, describing the 3D organisation of large macromolecules is an increasing, but challenging, necessity for structural biologists; such analyses require the ability to consistently screen large numbers of crystals, which would be very time-consuming and unreliable with more traditional human-driven techniques, making MASSIF a necessary improvement. However, interpretation of the 3D arrangement of the three domains of NtrX can only be performed by humans, so the final results will come later.<\/p>\n\n\n