Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of m-cresol

被引：2

作者：

Karavassili, Fotini ^{[1
]}

Valmas, Alexandros ^{[1
]}

Dimarogona, Maria ^{[2
]}

Giannopoulou, Anastasia E. ^{[1
]}

Fili, Stavroula ^{[1
]}

Norrman, Mathias ^{[3
]}

Schluckebier, Gerd ^{[3
]}

Beckers, Detlef ^{[4
]}

Fitch, Andrew N. ^{[5
]}

Margiolaki, I. ^{[1
]}

机构：

[1] Univ Patras, Dept Biol, Patras 26500, Greece

[2] Univ Patras, Dept Chem Engn, Patras 26500, Greece

[3] Novo Nordisk AS, Diabet Prot Engn, Novo Nordisk Pk, DK-2760 Malov, Denmark

[4] Malvern Panalyt BV, Lelyweg 1, NL-7602 Almelo, Netherlands

[5] European Synchrotron Radiat Facil, BP 220, F-38043 Grenoble 9, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2020年 / 76卷

关键词：

single-crystal diffraction; powder diffraction; synchrotron radiation; polymorphism; human insulin; m-cresol; diabetes mellitus; POWDER DIFFRACTION; MONOCLINIC CRYSTAL; PROTEIN CRYSTALS; LIGAND-BINDING; ZINC; STABILITY; HEXAMER; PHENOL; THIOCYANATE; REFINEMENT;

D O I：

10.1107/S2059798320002545

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

In this study, the first crystal structure of a novel crystal form of human insulin bound to meta-cresol in an acidic environment is reported. The combination of single-crystal and powder X-ray diffraction crystallography led to the detection of a previously unknown monoclinic phase (P2(1)). The structure was identified from the powder patterns and was solved using single-crystal diffraction data at 2.2 angstrom resolution. The unit-cell parameters at pH 6.1 are a = 47.66, b = 70.36, c = 84.75 angstrom, beta = 105.21 degrees. The structure consists of two insulin hexamers per asymmetric unit. The potential use of this insulin form in microcrystalline drugs is discussed.

引用

页码：366 / 374

页数：9

共 69 条

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[Anonymous], 1997, An introduction to hydrogen bonding

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