Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex. / Pitchai, Ganesha P; Hickson, Ian D; Streicher, Werner; Montoya, Guillermo; Mesa, Pablo.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. 72, No. 8, 08.2016, p. 646-651.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Pitchai, GP, Hickson, ID, Streicher, W, Montoya, G & Mesa, P 2016, 'Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, vol. 72, no. 8, pp. 646-651. https://doi.org/10.1107/S2053230X16010724

APA

Pitchai, G. P., Hickson, I. D., Streicher, W., Montoya, G., & Mesa, P. (2016). Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 72(8), 646-651. https://doi.org/10.1107/S2053230X16010724

Vancouver

Pitchai GP, Hickson ID, Streicher W, Montoya G, Mesa P. Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2016 Aug;72(8):646-651. https://doi.org/10.1107/S2053230X16010724

Author

Pitchai, Ganesha P ; Hickson, Ian D ; Streicher, Werner ; Montoya, Guillermo ; Mesa, Pablo. / Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex. In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2016 ; Vol. 72, No. 8. pp. 646-651.

Bibtex

@article{7b69fef39096444780da71e09104850b,
title = "Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex",
abstract = "Chromosome integrity depends on DNA structure-specific processing complexes that resolve DNA entanglement between sister chromatids. If left unresolved, these entanglements can generate either chromatin bridging or ultrafine DNA bridging in the anaphase of mitosis. These bridge structures are defined by the presence of the PICH protein, which interacts with the BEND3 protein in mitosis. To obtain structural insights into PICH-BEND3 complex formation at the atomic level, their respective NTPR and BD1 domains were cloned, overexpressed and crystallized using 1.56 M ammonium sulfate as a precipitant at pH 7.0. The protein complex readily formed large hexagonal crystals belonging to space group P6122, with unit-cell parameters a = b = 47.28, c = 431.58 {\AA} and with one heterodimer in the asymmetric unit. A complete multiwavelength anomalous dispersion (MAD) data set extending to 2.2 {\AA} resolution was collected from a selenomethionine-labelled crystal at the Swiss Light Source.",
author = "Pitchai, {Ganesha P} and Hickson, {Ian D} and Werner Streicher and Guillermo Montoya and Pablo Mesa",
year = "2016",
month = aug,
doi = "10.1107/S2053230X16010724",
language = "English",
volume = "72",
pages = "646--651",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "8",

}

RIS

TY - JOUR

T1 - Characterization of the NTPR and BD1 interacting domains of the human PICH-BEND3 complex

AU - Pitchai, Ganesha P

AU - Hickson, Ian D

AU - Streicher, Werner

AU - Montoya, Guillermo

AU - Mesa, Pablo

PY - 2016/8

Y1 - 2016/8

N2 - Chromosome integrity depends on DNA structure-specific processing complexes that resolve DNA entanglement between sister chromatids. If left unresolved, these entanglements can generate either chromatin bridging or ultrafine DNA bridging in the anaphase of mitosis. These bridge structures are defined by the presence of the PICH protein, which interacts with the BEND3 protein in mitosis. To obtain structural insights into PICH-BEND3 complex formation at the atomic level, their respective NTPR and BD1 domains were cloned, overexpressed and crystallized using 1.56 M ammonium sulfate as a precipitant at pH 7.0. The protein complex readily formed large hexagonal crystals belonging to space group P6122, with unit-cell parameters a = b = 47.28, c = 431.58 Å and with one heterodimer in the asymmetric unit. A complete multiwavelength anomalous dispersion (MAD) data set extending to 2.2 Å resolution was collected from a selenomethionine-labelled crystal at the Swiss Light Source.

AB - Chromosome integrity depends on DNA structure-specific processing complexes that resolve DNA entanglement between sister chromatids. If left unresolved, these entanglements can generate either chromatin bridging or ultrafine DNA bridging in the anaphase of mitosis. These bridge structures are defined by the presence of the PICH protein, which interacts with the BEND3 protein in mitosis. To obtain structural insights into PICH-BEND3 complex formation at the atomic level, their respective NTPR and BD1 domains were cloned, overexpressed and crystallized using 1.56 M ammonium sulfate as a precipitant at pH 7.0. The protein complex readily formed large hexagonal crystals belonging to space group P6122, with unit-cell parameters a = b = 47.28, c = 431.58 Å and with one heterodimer in the asymmetric unit. A complete multiwavelength anomalous dispersion (MAD) data set extending to 2.2 Å resolution was collected from a selenomethionine-labelled crystal at the Swiss Light Source.

U2 - 10.1107/S2053230X16010724

DO - 10.1107/S2053230X16010724

M3 - Journal article

C2 - 27487930

VL - 72

SP - 646

EP - 651

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - 8

ER -

ID: 164386001