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 Results for DC.creator="D." AND DC.creator="Ringe" in section 23.5.4 of volume F   page 1 of 2 pages.
Water structure in groups of well studied proteins
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4, pp. 808-814 [ doi:10.1107/97809553602060000894 ]
... molecules that are unique to one of the structures (Mattos & Ringe, 1996; Mattos, 2002; Mattos et al., 2006). 23.5.4.2.1. Elastase ... of functional groups likely to be found in larger ligands (Ringe, 1995; Mattos & Ringe, 1996; Mattos et al., 2006). Crystals of elastase ...

Protein kinase A
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2.5, p. 814 [ doi:10.1107/97809553602060000894 ]
Protein kinase A 23.5.4.2.5. Protein kinase A The comparative study of water molecules in seven different protein kinase A structures in complex with different ligands focused exclusively on the active site (Shaltiel et al., 1998). All of the structures were solved from isomorphous crystals to resolutions ranging from 2.0 to ...

Ribonuclease A
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2.4, pp. 813-814 [ doi:10.1107/97809553602060000894 ]
... Overall structure of RNase A. The overall structure of the d(CpA) complex of RNase A is shown as a ribbon ... conserved water molecules are shown as white spheres and the d(CpA) inhibitor in black. The three helices are labelled H1 ... Proteins Struct. Funct. Bioinform. 76, 861-881. Zegers, I., Maes, D., Dao-Thi, M.-H., Poortmans, F., Palmer, R. & Wyns, ...

Ribonuclease T1
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2.3, p. 813 [ doi:10.1107/97809553602060000894 ]
Ribonuclease T1 23.5.4.2.3. Ribonuclease T1 A group of four crystal structures of ribonuclease T1 in complex with guanosine, guanosine-2'-phosphate, guanylyl-2',5'-guanosine and vanadate were used for an analysis of conserved water positions that contribute to the structural stabilization of the protein (Malin et al., 1991). The ...

T4 lysozyme
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2.2, pp. 812-813 [ doi:10.1107/97809553602060000894 ]
T4 lysozyme 23.5.4.2.2. T4 lysozyme Over 150 mutants of T4 lysozyme have been studied to date, and, for the majority of these, the crystal structures are available. Although most of the mutant structures crystallize isomorphously to the wild type, many of them provide a view of the molecule in different crystal ...

Elastase
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2.1, pp. 809-812 [ doi:10.1107/97809553602060000894 ]
... of functional groups likely to be found in larger ligands (Ringe, 1995; Mattos & Ringe, 1996; Mattos et al., 2006). Crystals of elastase cross ... 5-hexene-1,2-diol (Mattos et al., 2006; Mattos & Ringe, 1996). In general, the crystals did not diffract ...

Multiple crystal structures of the same protein
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.2, pp. 809-814 [ doi:10.1107/97809553602060000894 ]
... molecules that are unique to one of the structures (Mattos & Ringe, 1996; Mattos, 2002; Mattos et al., 2006). 23.5.4.2.1. Elastase ... of functional groups likely to be found in larger ligands (Ringe, 1995; Mattos & Ringe, 1996; Mattos et al., 2006). Crystals of elastase ...

Legume lectin family
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.1.2, pp. 808-809 [ doi:10.1107/97809553602060000894 ]
... Langhorst, U., De Vos, S., Decanniere, K., Bouckaert, J., Maes, D., Transue, T. R. & Steyaert, J. (1999). Conserved water molecules ...

Serine proteases of the trypsin family
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.1.1, p. 808 [ doi:10.1107/97809553602060000894 ]
Serine proteases of the trypsin family 23.5.4.1.1. Serine proteases of the trypsin family The serine proteases have an especially large number of buried water molecules. Using a probe sphere of radius 1.4, an iterative procedure was used to delete all accessible surface waters for each structure of chymotrypsin, chymotrypsinogen, trypsin, trypsinogen ...

Crystal structures of homologous proteins
Mattos, C. and Ringe, D.  International Tables for Crystallography (2012). Vol. F, Section 23.5.4.1, pp. 808-809 [ doi:10.1107/97809553602060000894 ]
... Langhorst, U., De Vos, S., Decanniere, K., Bouckaert, J., Maes, D., Transue, T. R. & Steyaert, J. (1999). Conserved water molecules ...

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