On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.

By C. Mueller-Dieckmann, S. Panjikar, A. Schmidt, S. Mueller, J. Kuper, A. Geerlof, M. Wilmanns, R. Singh, Paul A. Tucker, M. Weiss. 2007

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Using SAD data in Phaser (2011, neutral): “In collaboration with Manfred Weiss and Christoph Mueller-Dieckmann, we are looking at the 23 data sets that they described earlier (Mueller-Dieckmann et al., 2007).”
Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin (2012, background): “Within this module the students learn how to collect X-ray diffraction data for de novo structure solutions, like MAD, S-SAD, SIRAS and UV-RIP, of several proteins of choice with hands-on-experiences using all of our MX beamlines.”
Introduction to phasing (2010, background): “D66, 325–338 Taylor Introduction to phasing 333 containing anomalous scatterers such as S, P, Ca, Xe, Cl or Zn (Mueller-Dieckmann et al., 2007).”
Insights from soft X-rays: the chlorine and sulfur sub-structures of a CK2α/DRB complex (2008, background): “Our anomalous dispersion study with a hsCK2a/DRB complex crystal confirms a previous study [4] with 19 different proteins that many hidden ions can be detected in protein crystal structures if soft X-rays are consequently applied.”
Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride (2009, background): “1 A, where a weak anomalous contribution from Cl − is expecte”