Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.

By G. Guncar, Ivica Klemenčič, Boris Turk, Vito Turk, A. Karaoglanovic-Carmona, Luiz Juliano, Dušan Turk. 2000

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Towards automated crystallographic structure refinement with phenix.refine (2012, background): “Other map types can also be output, such as average kick maps (AK maps; Guncar et al., 2000; Turk, 2007; Pražnikar et al., 2009) and B-factor sharpened maps (see Brunger et al., 358 Afonine et al. phenix.refine Acta Cryst.”
Cysteine cathepsins: From structure, function and regulation to new frontiers (2011, background): “L (1icf) [74], cathepsin S (1glo) [72], cathepsin V (1fh0) [69], cathepsin X (1ef7) [68],”
FEM: feature-enhanced map (2014, methodology): “This approach is also the basis of kick maps (Gunčar et al., 2000; Turk, 2013).”
Polder maps: improving OMIT maps by excluding bulk solvent (2017, background): “Various kinds of OMIT maps have been proposed (Bhat, 1988; Hodel et al., 1992; Vellieux & Dijkstra, 1997; Gunčar et al., 2000; Terwilliger, Grosse-Kunstleve, Afonine, Moriarty, Adams et al., 2008; Pražnikar et al., 2009).”