Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12

O V  Moroz; A A  Antson; G G  Dodson; K S  Wilson; I  Skibshoj; E M  Lukanidin; I B  Bronstein

Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12

O V Moroz, A A Antson, G G Dodson, K S Wilson, I Skibshoj, E M Lukanidin, I B Bronstein

Chemistry

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

Abstract

S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 Angstrom. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 Angstrom resolution and complete X-ray data have been collected to 2.5 Angstrom on a conventional laboratory source.

Original language	English
Pages (from-to)	189-191
Number of pages	3
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	56
Publication status	Published - Feb 2000

Keywords

CALGRANULIN-C
PIG GRANULOCYTES
FAMILY
CAAF1
MRP14
MODE
P6

Cite this

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title = "Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12",

abstract = "S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 Angstrom. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 Angstrom resolution and complete X-ray data have been collected to 2.5 Angstrom on a conventional laboratory source.",

keywords = "CALGRANULIN-C, PIG GRANULOCYTES, FAMILY, CAAF1, MRP14, MODE, P6",

author = "Moroz, {O V} and Antson, {A A} and Dodson, {G G} and Wilson, {K S} and I Skibshoj and Lukanidin, {E M} and Bronstein, {I B}",

year = "2000",

month = feb,

language = "English",

volume = "56",

pages = "189--191",

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

issn = "0907-4449",

publisher = "International Union of Crystallography",

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TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12

AU - Moroz, O V

AU - Antson, A A

AU - Dodson, G G

AU - Wilson, K S

AU - Skibshoj, I

AU - Lukanidin, E M

AU - Bronstein, I B

PY - 2000/2

Y1 - 2000/2

N2 - S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 Angstrom. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 Angstrom resolution and complete X-ray data have been collected to 2.5 Angstrom on a conventional laboratory source.

AB - S100A12, a member of the calgranulin family, isolated from human blood, has been crystallized by vapour diffusion in the presence of Ca2+. Crystals belong to the space group R3 with unit-cell dimensions a = b = 99.6 c = 64.2 Angstrom. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 Angstrom resolution and complete X-ray data have been collected to 2.5 Angstrom on a conventional laboratory source.

KW - CALGRANULIN-C

KW - PIG GRANULOCYTES

KW - FAMILY

KW - CAAF1

KW - MRP14

KW - MODE

KW - P6

M3 - Article

SN - 0907-4449

VL - 56

SP - 189

EP - 191

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

ER -