WHERE FREEDOM IS GIVEN, LIBERTIES ARE TAKEN

[21] Laskowski, MacArthur, Thornton, Evaluation of protein coordinate sets, From First Map to Final Model, pp. 149-159, (1994)

[22] Kleywegt, Jones, Et al., Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid, Structure, 2, pp. 1241-1258, (1994)

[23] Jones, Thirup, Using known substructures in protein model building and crystallography, EMBO J, 5, pp. 819-822, (1986)

[24] Schneider, Lindqvist, Lundqvist, Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 å resolution, J. Mol. Biol, 211, pp. 989-1008, (1990)

[25] Lundqvist, Schneider, Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate, J. Biol. Chem, 266, pp. 12604-12611, (1991)

[26] Sinning, Jones, Et al., Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes, J. Mol. Biol, 232, pp. 192-212, (1993)

[27] Cameron, Jones, Et al., Structural analysis of human alpha class glutathione transferase A1-1, in the apo form and in complexes with ethacrynic acid and its glutathione conjugate, Structure, 3, (1995)

[28] Korn, Rose, Torsion angle differences as a means of pinpointing local polypeptide chain trajectory changes for identical proteins in different conformational states, Protein Eng, 7, pp. 961-967, (1994)

[29] Zou, Mowbray, An evaluation of the use of databases in protein structure refinement, Acta Crystallographica Section D Biological Crystallography, 50, pp. 237-249, (1994)

[30] Rees, Largest likely values for R factors calculated after phase refinement by non-crystallographic symmetry averaging, Acta Crystallographica Section A Foundations of Crystallography, 39, pp. 916-920, (1983)

[21] Laskowski, MacArthur, Thornton, Evaluation of protein coordinate sets, From First Map to Final Model, pp. 149-159, (1994)

[22] Kleywegt, Jones, Et al., Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid, Structure, 2, pp. 1241-1258, (1994)

[23] Jones, Thirup, Using known substructures in protein model building and crystallography, EMBO J, 5, pp. 819-822, (1986)

[24] Schneider, Lindqvist, Lundqvist, Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 å resolution, J. Mol. Biol, 211, pp. 989-1008, (1990)

[25] Lundqvist, Schneider, Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate, J. Biol. Chem, 266, pp. 12604-12611, (1991)

[26] Sinning, Jones, Et al., Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes, J. Mol. Biol, 232, pp. 192-212, (1993)

[27] Cameron, Jones, Et al., Structural analysis of human alpha class glutathione transferase A1-1, in the apo form and in complexes with ethacrynic acid and its glutathione conjugate, Structure, 3, (1995)

[28] Korn, Rose, Torsion angle differences as a means of pinpointing local polypeptide chain trajectory changes for identical proteins in different conformational states, Protein Eng, 7, pp. 961-967, (1994)

[29] Zou, Mowbray, An evaluation of the use of databases in protein structure refinement, Acta Crystallographica Section D Biological Crystallography, 50, pp. 237-249, (1994)

[30] Rees, Largest likely values for R factors calculated after phase refinement by non-crystallographic symmetry averaging, Acta Crystallographica Section A Foundations of Crystallography, 39, pp. 916-920, (1983)