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  • Structural studies of human insulin cocrystallized with phenol or resorcinol via powder diffraction.

Structural studies of human insulin cocrystallized with phenol or resorcinol via powder diffraction.

Acta crystallographica. Section D, Biological crystallography (2012-11-16)
Fotini Karavassili, Anastasia E Giannopoulou, Eleni Kotsiliti, Lisa Knight, Mathias Norrman, Gerd Schluckebier, Lene Drube, Andrew N Fitch, Jonathan P Wright, Irene Margiolaki
ABSTRACT

The effects of the ligands phenol and resorcinol on the crystallization of human insulin have been investigated as a function of pH. Powder diffraction data were used to characterize several distinct polymorphic forms. A previously unknown polymorph with monoclinic symmetry (P2(1)) was identified for both types of ligand with similar characteristics [the unit-cell parameters for the insulin-resorcinol complex were a = 114.0228 (8), b = 335.43 (3), c = 49.211 (6) Å, β = 101.531 (8)°].

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Resorcinol, ≥98%, FG
Sigma-Aldrich
Resorcinol, ACS reagent, ≥99.0%
Sigma-Aldrich
Resorcinol, meets analytical specification of Ph. Eur., BP, 98.5-100.5% (calc. to the dried substance)
Sigma-Aldrich
Resorcinol, ReagentPlus®, 99%
Sigma-Aldrich
Resorcinol, BioXtra, ≥99%
Supelco
Resorcinol, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland