The long-wavelength macromolecular crystallography beamline I23 is a unique facility for solving the crystallographic phase problem, using the small anomalous signals from sulphur or phosphorus which are present in native protein or RNA/DNA crystals. This is of increased importance for projects where protein labelling to introduce anomalous scatterers is not feasible. In addition, the beamline's wavelength range provides access to the M-edges of elements, with huge anomalous signals offering new opportunities for phasing large molecular complexes.
The unique wavelength range also allows identification and location of lighter atoms of biological relevance such as Cl, K and Ca and assistance with low-resolution model building by locating P or S atom positions.
I23 complements the existing suite of five MX beamlines at Diamond being optimised for operation in the wavelength range from 1.5 to 4 Å. The in-vacuum experimental end station minimizes absorption and scattering effects. A large semi-cylindrical detector allows measurements of a large range of diffraction angles and a multi-axis goniometer is available for crystal alignment and orientation. An X-ray tomography setup will be integrated into the beamline end station to obtain the crystal shape and volume as a basis of an analytical absorption correction.
First successful data has been collected demonstrating the advantages of in-vacuum MX [1,2,3]. The beamline has welcomed first users in February 2016 and is now in an advanced commissioning phase.
We have already solved a number of difficult structures, our main effort is now towards making the beamline a user facility. At the moment we are accepting projects in a collaborative friendly user mode. Please get into touch if you have an interesting project which can profit from I23's unique capabilities.
 A. Wagner, R. Duman, K. Henderson, V. Mykhaylyk In-vacuum long-wavelength macromolecular crystallography Acta Cryst. D72 (2016) 430-439.
 A. F. Brent, G. Mann, W. E. Houssen, V. Mykhaylyk, R. Duman, L. Thomas, M. Jaspars, A. Wagner, J. H. Naismith Structure of the cyanobactin oxidase ThcOx from Cyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD Acta Cryst. D72 (2016) 1174-1180.
 K. Bountra, G. Hagelueken, H. G. Choudhury, V. Corradi, K. El Omari, A. Wagner, I. Mathavan, S. Zirah, W. Y. Wahlgren, D. P. Tieleman, O. Schiemann, S. Rebuffat, K. Beis Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD EMBO J. (2017) in press
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