STRUCTURE OF THE PIG INSULIN DIMER IN THE CUBIC-CRYSTAL

J Badger; M R Harris; C D Reynolds; A C Evans; E J Dodson; G G Dodson; A C T North

STRUCTURE OF THE PIG INSULIN DIMER IN THE CUBIC-CRYSTAL

J Badger, M R Harris, C D Reynolds, A C Evans, E J Dodson, G G Dodson, A C T North

Psychology

Research output: Contribution to journal › Article › peer-review

Abstract

Atomic coordinates for pig insulin in the cubic crystal have been refined by reciprocal-space methods to an R factor of 0.173 for data between 10.0 and 1.7 angstrom resolution with structure-factor amplitudes greater than two standard deviations. Stereochemical parameters for the refined model are close to standard values and the estimated error in the positions of well-ordered atoms is about 0.1 angstrom. Residues directly involved in the formation of the exact (crystallographic) cubic insulin dimer are oriented similarly to those in the non-crystallographic 2Zn insulin dimer. Other residues, which make different molecular contacts in the different crystal forms, have locally altered conformations. The cubic insulin molecule is significantly more similar to one of the two independent molecules in the 2Zn insulin dimer than the other. This more similar molecule is expected to be the more stable conformer.

Original language	English
Pages (from-to)	127-136
Number of pages	10
Journal	ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE
Volume	47
Publication status	Published - 1 Feb 1991

Keywords

INDEPENDENTLY REFINED MODELS
LEAST-SQUARES
SOLVENT MOLECULES
PROTEIN-STRUCTURE
2-ZINC INSULIN
X-RAY
HEXAMER
RESOLUTION
OCCUPANCY

Cite this

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title = "STRUCTURE OF THE PIG INSULIN DIMER IN THE CUBIC-CRYSTAL",

abstract = "Atomic coordinates for pig insulin in the cubic crystal have been refined by reciprocal-space methods to an R factor of 0.173 for data between 10.0 and 1.7 angstrom resolution with structure-factor amplitudes greater than two standard deviations. Stereochemical parameters for the refined model are close to standard values and the estimated error in the positions of well-ordered atoms is about 0.1 angstrom. Residues directly involved in the formation of the exact (crystallographic) cubic insulin dimer are oriented similarly to those in the non-crystallographic 2Zn insulin dimer. Other residues, which make different molecular contacts in the different crystal forms, have locally altered conformations. The cubic insulin molecule is significantly more similar to one of the two independent molecules in the 2Zn insulin dimer than the other. This more similar molecule is expected to be the more stable conformer.",

keywords = "INDEPENDENTLY REFINED MODELS, LEAST-SQUARES, SOLVENT MOLECULES, PROTEIN-STRUCTURE, 2-ZINC INSULIN, X-RAY, HEXAMER, RESOLUTION, OCCUPANCY",

author = "J Badger and Harris, {M R} and Reynolds, {C D} and Evans, {A C} and Dodson, {E J} and Dodson, {G G} and North, {A C T}",

year = "1991",

month = feb,

day = "1",

language = "English",

volume = "47",

pages = "127--136",

journal = "ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE",

issn = "0108-7681",

publisher = "International Union of Crystallography",

}

TY - JOUR

T1 - STRUCTURE OF THE PIG INSULIN DIMER IN THE CUBIC-CRYSTAL

AU - Badger, J

AU - Harris, M R

AU - Reynolds, C D

AU - Evans, A C

AU - Dodson, E J

AU - Dodson, G G

AU - North, A C T

PY - 1991/2/1

Y1 - 1991/2/1

N2 - Atomic coordinates for pig insulin in the cubic crystal have been refined by reciprocal-space methods to an R factor of 0.173 for data between 10.0 and 1.7 angstrom resolution with structure-factor amplitudes greater than two standard deviations. Stereochemical parameters for the refined model are close to standard values and the estimated error in the positions of well-ordered atoms is about 0.1 angstrom. Residues directly involved in the formation of the exact (crystallographic) cubic insulin dimer are oriented similarly to those in the non-crystallographic 2Zn insulin dimer. Other residues, which make different molecular contacts in the different crystal forms, have locally altered conformations. The cubic insulin molecule is significantly more similar to one of the two independent molecules in the 2Zn insulin dimer than the other. This more similar molecule is expected to be the more stable conformer.

AB - Atomic coordinates for pig insulin in the cubic crystal have been refined by reciprocal-space methods to an R factor of 0.173 for data between 10.0 and 1.7 angstrom resolution with structure-factor amplitudes greater than two standard deviations. Stereochemical parameters for the refined model are close to standard values and the estimated error in the positions of well-ordered atoms is about 0.1 angstrom. Residues directly involved in the formation of the exact (crystallographic) cubic insulin dimer are oriented similarly to those in the non-crystallographic 2Zn insulin dimer. Other residues, which make different molecular contacts in the different crystal forms, have locally altered conformations. The cubic insulin molecule is significantly more similar to one of the two independent molecules in the 2Zn insulin dimer than the other. This more similar molecule is expected to be the more stable conformer.

KW - INDEPENDENTLY REFINED MODELS

KW - LEAST-SQUARES

KW - SOLVENT MOLECULES

KW - PROTEIN-STRUCTURE

KW - 2-ZINC INSULIN

KW - X-RAY

KW - HEXAMER

KW - RESOLUTION

KW - OCCUPANCY

M3 - Article

SN - 0108-7681

VL - 47

SP - 127

EP - 136

JO - ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE

JF - ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE

ER -