Preliminary X-ray crystallographic analysis of a Ca2+-binding protein human S100A1

Z. Wang; H. Zhang; Y. Ding; G. Wang; X. Wang; S. Ye; M. Bartlam; H. Tang; Y. Liu; F. Jiang; R. Barraclough; P. S. Rudland; Z. Rao

doi:10.1107/S0907444901005273

Preliminary X-ray crystallographic analysis of a Ca²⁺-binding protein human S100A1

Z. Wang
, H. Zhang
, Y. Ding
, G. Wang
, X. Wang
, S. Ye
, M. Bartlam
, H. Tang
, Y. Liu
, F. Jiang
, R. Barraclough
, P. S. Rudland
, Z. Rao^*

^*Corresponding author for this work

Tsinghua University

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

5 Scopus citations

Abstract

S100A1, a Ca²⁺-binding protein from the S100 protein family, has been crystallized by the vapour-diffusion method using polyethylene glycol 4000 as the precipitant at pH 8.5. The crystal belongs to space group P6₃. The unit-cell parameters are a = b = 57.3, c = 104.7 Å. There appear to be two S100A1 molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and diffract to 2.6 Å resolution in-house.

Original language	English
Pages (from-to)	882-883
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	6
DOIs	https://doi.org/10.1107/S0907444901005273
State	Published - 2001
Externally published	Yes

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@article{415f3a8df2f84b9eaa3f0ee29d40cc3c,

title = "Preliminary X-ray crystallographic analysis of a Ca2+-binding protein human S100A1",

abstract = "S100A1, a Ca2+-binding protein from the S100 protein family, has been crystallized by the vapour-diffusion method using polyethylene glycol 4000 as the precipitant at pH 8.5. The crystal belongs to space group P63. The unit-cell parameters are a = b = 57.3, c = 104.7 {\AA}. There appear to be two S100A1 molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and diffract to 2.6 {\AA} resolution in-house.",

author = "Z. Wang and H. Zhang and Y. Ding and G. Wang and X. Wang and S. Ye and M. Bartlam and H. Tang and Y. Liu and F. Jiang and R. Barraclough and Rudland, \{P. S.\} and Z. Rao",

year = "2001",

doi = "10.1107/S0907444901005273",

language = "英语",

volume = "57",

pages = "882--883",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

number = "6",

}

TY - JOUR

T1 - Preliminary X-ray crystallographic analysis of a Ca2+-binding protein human S100A1

AU - Wang, Z.

AU - Zhang, H.

AU - Ding, Y.

AU - Wang, G.

AU - Wang, X.

AU - Ye, S.

AU - Bartlam, M.

AU - Tang, H.

AU - Liu, Y.

AU - Jiang, F.

AU - Barraclough, R.

AU - Rudland, P. S.

AU - Rao, Z.

PY - 2001

Y1 - 2001

N2 - S100A1, a Ca2+-binding protein from the S100 protein family, has been crystallized by the vapour-diffusion method using polyethylene glycol 4000 as the precipitant at pH 8.5. The crystal belongs to space group P63. The unit-cell parameters are a = b = 57.3, c = 104.7 Å. There appear to be two S100A1 molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and diffract to 2.6 Å resolution in-house.

AB - S100A1, a Ca2+-binding protein from the S100 protein family, has been crystallized by the vapour-diffusion method using polyethylene glycol 4000 as the precipitant at pH 8.5. The crystal belongs to space group P63. The unit-cell parameters are a = b = 57.3, c = 104.7 Å. There appear to be two S100A1 molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and diffract to 2.6 Å resolution in-house.

UR - https://www.scopus.com/pages/publications/14344284943

U2 - 10.1107/S0907444901005273

DO - 10.1107/S0907444901005273

M3 - 文章

C2 - 11375516

AN - SCOPUS:14344284943

SN - 0907-4449

VL - 57

SP - 882

EP - 883

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 6

ER -

Preliminary X-ray crystallographic analysis of a Ca²⁺-binding protein human S100A1

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