PROTOCOLS Complex production Expression in insect cells: reagents and protocols for multi-protein complex expression using baculovirus vectors. J Struct Biol. 2010 Feb 21. [Epub ahead of print] PMID: 2017884 New eukaryotic expression tools for protein complex production. Trowitzsch, S., Bieniossek, C., Nie, Y., Garzoni, F., Berger, I. ACEMBL: a versatile and automatable system for protein-complex expression in Escherichia coli. Nat Methods. 2009 Jun;6(6):447-50. Epub 2009 May 3. PMID: 19412171 Automated unrestricted multigene recombineering for multiprotein complex production. Bieniossek C, Nie Y, Frey D, Olieric N, Schaffitzel C, Collinson I, Romier C, Berger P, Richmond TJ, Steinmetz MO, Berger I. MultiBac: reagents and protocols for multi-protein complex expression using baculovirus vectors. J Struct Funct Genomics. 2009 Mar;10(1):37-46. Epub 2008 Nov 14. PMID: 19009368 Towards eukaryotic structural complexomics. Bieniossek C, Berger I. ESPRIT: automated library-based method for mapping and soluble expression of protein domains J Struct Biol. 2010 Mar 4. [Epub ahead of print] PMID: 20206698 ESPRIT: An automated, library-based method for mapping and soluble expression of protein domains from challenging targets Yumerefendi, H., Tarendeau, F., Mas, P. & Hart, DJ Mass Spectrometry & Electron Microscopy Grafix: method that improves sample quality for structure determination by single-particle electron cryomicroscopy (cryo-EM). GraFix uses a glycerol gradient centrifugation step in which the complexes are centrifuged into an increasing concentration of a chemical fixation reagent to prevent aggregation and to stabilize individual macromolecules. Nat Methods. 2008 Jan;5(1):53-5. Epub 2007 Dec 23. PMID: 18157137 GraFix: sample preparation for single-particle electron cryomicroscopy. Kastner B, Fischer N, Golas MM, Sander B, Dube P, Boehringer D, Hartmuth K, Deckert J, Hauer F, Wolf E, Uchtenhagen H, Urlaub H, Herzog F, Peters JM, Poerschke D, Lührmann R, Stark H. Ion mobility-mass spectrometry approach capable to distinguish the overall subunit architecture of protein complexes. The approach relies on the simultaneous measurement in the gas phase of the mass and size of intact assemblies and sub-complexes. These data are then used as restraints to generate topological models of protein complexes. Structure. 2009 Sep 9;17(9):1235-43. PMID: 19748344 Subunit architecture of multiprotein assemblies determined using restraints from gas-phase measurements. Pukala TL, Ruotolo BT, Zhou M, Politis A, Stefanescu R, Leary JA, Robinson CV. Nuclear Magnetic Resonance Protocol for NMR-Based structure determination of Protein Complexes in solution Angew Chem Int Ed Engl. 2010 Mar 8;49(11):1967-70. PMID: 20148424 An Efficient Protocol for NMR-Based Structure Determination of Protein Complexes in Solution Simon B, Madl T, Mackereth CD, Nilges M, Sattler M A structure refinement protocol combing NMR residual dipolar couplings and small angle scattering restraints J Biomol NMR. 2008 Aug;41(4):199-208. Epub 2008 Aug 1. A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints. Gabel F, Simon B, Nilges M, Petoukhov M, Svergun D, Sattler M. PMID: 18670889