MX2 Beamline

The MX2 beamline is an experimental station dedicated to Macromolecular Crystallography in the hard x-rays energy range (5 to 15 keV) with maximum flux at 8.5 keV. The station is available for conventional single wavelength data collection as well as for Single and Multiple-wavelength Anomalous Diffraction (SAD/MAD) experiments. 

MX2 operates on a 2.0 T hybrid 30-pole wiggler and its optical layout includes collimating mirror, Si(111) double-crystal monochromator and toroidal bendable mirror. The beamline is equipped with PILATUS2M detector from Dectris.

The research projects developed at the MX2 beamline yield precise information about the atomic constitution and shape of macromolecules, such as enzymes and membrane-bound proteins, the building blocks of life inside and outside living cells. This information can lead to a fuller understanding of the biological processes carried by these molecules and by consequence, to the development of new and more efficient medications, cosmetics, biofuels and biomaterials.

Starting from a protein crystal, researchers can obtain information about the three-dimensional shape of the protein, and also run screening studies, where atomic details of small molecules that interact with the protein under study can reveal new avenues for the design of inhibitors. These studies can reveal the detailed mechanisms of the interactions between substrates and enzymes, suggesting improvement or inhibition routes that can guide synthetic or natural products chemists in the development of new commodities.


For more information on this beamline, contact us.


The following experimental techniques and setups are available to users in this beamline. To learn more about the techniques’ limitations and requirements (sample, environment, etc.) contact the beamline coordinator before submitting your proposal.


The station is available for conventional single wavelength data collection as well as for Single and Multiple-wavelength Anomalous Diffraction (SAD/MAD) experiments.

Recent publications using this setup:

  • Structural basis for dimer formation of the CRISPR-associated protein Csm2 of Thermotoga maritima. Gallo, G., Gilles, A., Rangel, G., Zelanis, A., Mori, M. A., Campos, C. B., Wurtele, M. FEBS Journal, v. 283, n. 4, p. 694-703, 2016.
  • Structural analysis of a Dioclea sclerocarpa lectin: Study on the vasorelaxant properties of Dioclea lectins. Barroso- Neto, I. L., Delatorre, P., Teixeira, C. S., Correia, J. L. A., Cajazeiras, J. B., Pereira, R. I., Nascimento, K. S., Laranjeira, E. P. P., Pires, A. F., Assreuy, A. M. S., Rocha, B. A. M., Cavada, B. S.
, International Journal of Biological Macromolecules, v. 82, p. 464- 470, 2016.
  • Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa. Matsuyama, B. Y., Krasteva, P. V., Baraquet, C., Harwood, C. S., Sondermann, H., Navarro, M. V. A. S. Proceedings of the National Academy of Sciences USA, v.113, n. 2, p. E209-E218, 2016.


Element Type Position [m] Description
SOURCE Insertion Device 0.00 Insertion Device W01A, 2.0 T hybrid 30-pole Wiggler, 22 mm minimal gap
M1 Cylindrical Vertical Collimating Mirror 11.00 Rh coated ULE glass, θ=4 mrad
Mono Double Crystal Monochromator 14.26 Water-cooled Si(111)
M2 Toroidal Horizontal and Vertical Focusing Mirror 16.00 Rh coated silicon, θ=4 mrad, mechanical bender


Parameter Value Condition
Energy range [keV] 5-15 Si(111)
Energy resolution [E/E] 10-4 Si(111)
Beam size at sample [µm2, FWHM] 150 x 500 at 8.5 keV
Beam divergence at sample [mrad2, FWHM] 3 at 8.5 keV
Flux density at sample [ph/s/mm2] 1011 at 8.5 keV


Instrument Type Model Manufacturer Specifications
Detector Area PILATUS2M 172 µm pixel, 1475 x 1679 pixel, 30 kHz frame rate Dectris
Diffractometer Data collection MarDTB Phi and theta rotations. Ionizations chambers, slits, shutter and sample holding. Detector translation range 100 to 350 mm. Rayonics
Cryostats Nitrogen Cryojet XL Sample cooling at 100 Kelvin. Oxford
Detector Fluorescence X-123SDD Si drift diode (SDD). Energy resolution 125 to 140 eV FWHM at 5.9 KeV. Maximum count rate 4 x 106 s-1 Channels number 8. Communication via Ethernet Amptek


The optical controls are done through EPICS (Experimental Physics and Industrial Control System), running on a control system called PXI from National Instruments. The experimental control and data collection with the Pilatus 2M detector (Dectris) are done via a RedHat station running the Python based software MXCube. MXCube is the product of an international collaboration for the creation and development of a graphic interface for molecular crystallography beamlines (Gabadinho, J.et al.,2010, J. Synchrotron Rad. 17, 700-707). A mini-kappa goniometer and a robot for in-plate data collection are currently under commissioning.

There are also two machines with RedHat workstation to access one Virtual Machine with the following software applications available for data treatment: iMOSFLM (v1.0.5); HKL2000* (v0.98.695B); CCP4 PACKAGE; SHELX; HKL2MAP (v0.2); PHENIX (v1.7); CNS; COOT; PYMOL; SHARP.

Additional material concerning those software is linked below:

* The HKL-2000 program package available at the beamline is provided on the basis of scientific collaboration free of charge by the program Authors.

The use of the package should be referenced in publication as follows: Z. Otwinowski and W. Minor “Processing of X-ray Diffraction Data Collected in Oscillation Mode”, Methods in Enzymology, Volume 276: Macromolecular Crystallography, part A, p. 307-326, 1997, C.W. Carter, Jr. and R.M. Sweet, Eds., Academic Press.

Researchers who perform non-commercial research may freely use the program for data evaluation and processing while collecting data at the beamline. Researchers from institutions who want to use the program for data evaluation and processing for commercial purposes while collecting data on LNLS beamlines must have an appropriate HKL-2000 license. The license can be obtained from HKL Research, Inc.  The HKL-2000 package development is supported by the NIH grant GM-53163 to the laboratories of Drs. Zbyszek Otwinowski (Southwester Medical Center at Dallas) and Wladek Minor (University of Virginia).


Users are required to acknowledge the use of LNLS facilities in any paper, conference presentation, thesis and any other published material that uses data obtained in the execution of their proposal.


Additionally, in publications related to this facility, please cite the following publication.

GUIMARÃES, B. G.; SANFELICI, L.; NEUENSCHWANDER, R. T.; RODRIGUES, FL.; GRIZOLLI, W. C.; RAULIK, M. A.; PITON, J. R.; MEYER, B. C.; NASCIMENTO, A. S.; POLIKARPOV, I. The MX2 macromolecular crystallography beamline: a wiggler X-ray source at the LNLS. Journal of Synchrotron Radiation, 16: 69-75 (2009). doi:10.1107/S0909049508034870.

The Brazilian Synchrotron Light Laboratory [Laboratório Nacional de Luz Síncrotron (LNLS), Campinas, SP, Brazil] is the first commissioned synchrotron light source in the southern hemisphere. The first wiggler macromolecular crystallography beamline (MX2) at the LNLS has been recently constructed and brought into operation. Here the technical design, experimental set-up, parameters of the beamline and the first experimental results obtained at MX2 are described. The beamline operates on a 2.0 T hybrid 30-pole wiggler, and its optical layout includes collimating mirror, Si(111) double-crystal monochromator and toroidal bendable mirror. The measured flux density at the sample position at 8.7 eV reaches 4.8 x 10^{11} photons s^{-1} mm^{-2} (100 mA)^{-1}. The beamline is equipped with a MarResearch Desktop Beamline Goniostat (MarDTB) and 3 x 3 MarMosaic225 CCD detector, and is controlled by a customized version of the Blu-Ice software. A description of the first X-ray diffraction data sets collected at the MX2 LNLS beamline and used for macromolecular crystal structure solution is also provided.



Scientific publications produced with data obtained at the facilities of this beamline, and published in journals indexed by the Web of Science, are listed below.

Attention Users: Given the importance of the previous scientific results to the overall proposal evaluation process, users are strongly advised to check and update their publication record at the SAU Online website. 

Cabral, L. ;Persinoti, G. F.;Paixão, D. A. A.;Martins, M. P. ;Morais, M. A. B.de ;Chinaglia, M.;Domingues, M. N.;Sforça, M. L.;Pirolla, R. A. S. ;Generoso, W. C.;Santos, C. A.;Maciel, L. F. ;Terrapon, N. ;Lombard, V. ;Henrissat, B.;Murakami, M. T.. Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides, Nature Communications, v.13, n.1, p.629, 2022. DOI:10.1038/s41467-022-28310-y

Wegermann, C. A. ;Monzani, E. ;Casella, L. ;Ribeiro, M. A.;Bruzeguini, C. E. T. ;Vilcachagua, J. D. ;Costa, L. A. S. ;Ferreira, A. M. da C.. Unveiling geometrical isomers and tautomers of isatin-hydrazones by NMR spectroscopy, Journal of Molecular Structure, v.1250, n.2, p.131633, 2022. DOI:10.1016/j.molstruc.2021.131633

Fontana, L. A.;Rigolin, V. H.;Ribeiro, M. A.;Barros, W. P.;Megiatto Jr., J. D.. A synthetic tactic to substitute axial ligands in sterically demanding Ru(II)porphyrinates, Dalton Transactions, v.51, p. 9971-9977, 2022. DOI:10.1039/d2dt01095j

Liberato, M. V.;Ramos, B. M. C.;Tomazetto, G.;Crouch, L. I.;Silva, W. J. G. da ;Zeri, A. C. de M.;Bolam, D. N. ;Squina, F. M.. Unique properties of a Dictyostelium discoideum carbohydrate-binding module expand our understanding of CBM–ligand interactions, Journal of Biological Chemistry, v.298, n.5, p.101891, 2022. DOI:10.1016/j.jbc.2022.101891

Cornejo, H. E. L. ;Cenens, W. ;Favaro, D. C.;Sgro, G. G. ;Salinas, R. K.;Guzzo, C. R.;Farah, C. S.. The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri, PLoS Pathogens, v.17, n.8, p.e1009808, 2022. DOI:10.1371/journal.ppat.1009808

Gismene, C. ;Hernández González, J. E. ;Santisteban, A. R. N. ;Nascimento, A. F. Z.;Cunha, L. dos S. ;Moraes, F. R. de;Oliveira, C. L. P.;Oliveira, C. C. ;Provazzi, P. J. S. ;Pascutti, P. G.;Arni, R. K.;Mariutti, R. B.. Staphylococcus aureus Exfoliative Toxin E, Oligomeric State and Flip of P186: Implications for Its Action Mechanism, International Journal of Molecular Sciences, v.23, n.17, p.9857, 2022. DOI:10.3390/ijms23179857