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Crystallization and diffraction of an Lhx4–Isl2 complex.

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Crystallization and diffraction of an Lhx4–Isl2 complex. / Gadd, Morgan Stuart; Langley, David B; Guss, J Mitchell et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 2, 31.01.2009, p. 151-153.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Gadd, MS, Langley, DB, Guss, JM & Matthews, JM 2009, 'Crystallization and diffraction of an Lhx4–Isl2 complex.', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 65, no. 2, pp. 151-153. https://doi.org/10.1107/S1744309108043431

APA

Gadd, M. S., Langley, D. B., Guss, J. M., & Matthews, J. M. (2009). Crystallization and diffraction of an Lhx4–Isl2 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(2), 151-153. https://doi.org/10.1107/S1744309108043431

Vancouver

Gadd MS, Langley DB, Guss JM, Matthews JM. Crystallization and diffraction of an Lhx4–Isl2 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2009 Jan 31;65(2):151-153. doi: 10.1107/S1744309108043431

Author

Gadd, Morgan Stuart ; Langley, David B ; Guss, J Mitchell et al. / Crystallization and diffraction of an Lhx4–Isl2 complex. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2009 ; Vol. 65, No. 2. pp. 151-153.

Bibtex

@article{23a43903ad594e17b32c62406cbdca95,
title = "Crystallization and diffraction of an Lhx4–Isl2 complex.",
abstract = "A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P21, with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 {\AA}, β = 111.9°, and diffracted to 2.16 {\AA} resolution.",
author = "Gadd, {Morgan Stuart} and Langley, {David B} and Guss, {J Mitchell} and Matthews, {Jacqueline M}",
year = "2009",
month = jan,
day = "31",
doi = "10.1107/S1744309108043431",
language = "English",
volume = "65",
pages = "151--153",
journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",
issn = "1744-3091",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Crystallization and diffraction of an Lhx4–Isl2 complex.

AU - Gadd, Morgan Stuart

AU - Langley, David B

AU - Guss, J Mitchell

AU - Matthews, Jacqueline M

PY - 2009/1/31

Y1 - 2009/1/31

N2 - A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P21, with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 Å, β = 111.9°, and diffracted to 2.16 Å resolution.

AB - A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P21, with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 Å, β = 111.9°, and diffracted to 2.16 Å resolution.

U2 - 10.1107/S1744309108043431

DO - 10.1107/S1744309108043431

M3 - Journal article

VL - 65

SP - 151

EP - 153

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

SN - 1744-3091

IS - 2

ER -