6fj8
From Proteopedia
Structure of Thaumatin collected from an in situ crystal collected on ID30B at 12.7 keV.
Structural highlights
Function[THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedID30B is an undulator-based high-intensity, energy-tuneable (6.0-20 keV) and variable-focus (20-200 microm in diameter) macromolecular crystallography (MX) beamline at the ESRF. It was the last of the ESRF Structural Biology Group's beamlines to be constructed and commissioned as part of the ESRF's Phase I Upgrade Program and has been in user operation since June 2015. Both a modified microdiffractometer (MD2S) incorporating an in situ plate screening capability and a new flexible sample changer (the FlexHCD) were specifically developed for ID30B. Here, the authors provide the current beamline characteristics and detail how different types of MX experiments can be performed on ID30B (http://www.esrf.eu/id30b). ID30B - a versatile beamline for macromolecular crystallography experiments at the ESRF.,McCarthy AA, Barrett R, Beteva A, Caserotto H, Dobias F, Felisaz F, Giraud T, Guijarro M, Janocha R, Khadrouche A, Lentini M, Leonard GA, Lopez Marrero M, Malbet-Monaco S, McSweeney S, Nurizzo D, Papp G, Rossi C, Sinoir J, Sorez C, Surr J, Svensson O, Zander U, Cipriani F, Theveneau P, Mueller-Dieckmann C J Synchrotron Radiat. 2018 Jul 1;25(Pt 4):1249-1260. doi:, 10.1107/S1600577518007166. Epub 2018 Jun 27. PMID:29979188[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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