Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae

Rafael Molina; Ana González; Miriam Moscoso; Pedro García; Meike Stelter; Richard Kahn; Juan A Hermoso

doi:10.1107/S1744309107035865

Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae

Rafael Molina, Ana González, Miriam Moscoso, Pedro García, Meike Stelter, Richard Kahn, Juan A Hermoso

Protein Structure and Function Program

7 Citationer (Scopus)

Abstract

Choline-binding protein F (CbpF) is a modular protein that is bound to the pneumococcal cell wall through noncovalent interactions with choline moieties of the bacterial teichoic and lipoteichoic acids. Despite being one of the more abundant proteins on the surface, along with the murein hydrolases LytA, LytB, LytC and Pce, its function is still unknown. CbpF has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 49.13, b = 114.94, c = 75.69 A. A SAD data set from a Gd-HPDO3A-derivatized CbpF crystal was collected to 2.1 A resolution at the gadolinium L(III) absorption edge using synchrotron radiation.

Originalsprog	Engelsk
Tidsskrift	Acta Crystallographica Section F: Structural Biology Communications
Vol/bind	63
Udgave nummer	Pt 9
Sider (fra-til)	742-5
Antal sider	4
ISSN	2053-230X
DOI	https://doi.org/10.1107/S1744309107035865
Status	Udgivet - 1 sep. 2007

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10.1107/S1744309107035865

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Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae. / Molina, Rafael ; González, Ana; Moscoso, Miriam et al.

I: Acta Crystallographica Section F: Structural Biology Communications, Bind 63, Nr. Pt 9, 01.09.2007, s. 742-5.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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title = "Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae",

abstract = "Choline-binding protein F (CbpF) is a modular protein that is bound to the pneumococcal cell wall through noncovalent interactions with choline moieties of the bacterial teichoic and lipoteichoic acids. Despite being one of the more abundant proteins on the surface, along with the murein hydrolases LytA, LytB, LytC and Pce, its function is still unknown. CbpF has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 49.13, b = 114.94, c = 75.69 A. A SAD data set from a Gd-HPDO3A-derivatized CbpF crystal was collected to 2.1 A resolution at the gadolinium L(III) absorption edge using synchrotron radiation.",

keywords = "Bacterial Proteins/chemistry, Carrier Proteins/chemistry, Crystallization, Polymerase Chain Reaction, Recombinant Proteins/chemistry, Streptococcus pneumoniae/chemistry, Synchrotrons, X-Ray Diffraction",

author = "Rafael Molina and Ana Gonz{\'a}lez and Miriam Moscoso and Pedro Garc{\'i}a and Meike Stelter and Richard Kahn and Hermoso, {Juan A}",

year = "2007",

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T1 - Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae

AU - Molina, Rafael

AU - González, Ana

AU - Moscoso, Miriam

AU - García, Pedro

AU - Stelter, Meike

AU - Kahn, Richard

AU - Hermoso, Juan A

PY - 2007/9/1

Y1 - 2007/9/1

N2 - Choline-binding protein F (CbpF) is a modular protein that is bound to the pneumococcal cell wall through noncovalent interactions with choline moieties of the bacterial teichoic and lipoteichoic acids. Despite being one of the more abundant proteins on the surface, along with the murein hydrolases LytA, LytB, LytC and Pce, its function is still unknown. CbpF has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 49.13, b = 114.94, c = 75.69 A. A SAD data set from a Gd-HPDO3A-derivatized CbpF crystal was collected to 2.1 A resolution at the gadolinium L(III) absorption edge using synchrotron radiation.

AB - Choline-binding protein F (CbpF) is a modular protein that is bound to the pneumococcal cell wall through noncovalent interactions with choline moieties of the bacterial teichoic and lipoteichoic acids. Despite being one of the more abundant proteins on the surface, along with the murein hydrolases LytA, LytB, LytC and Pce, its function is still unknown. CbpF has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 49.13, b = 114.94, c = 75.69 A. A SAD data set from a Gd-HPDO3A-derivatized CbpF crystal was collected to 2.1 A resolution at the gadolinium L(III) absorption edge using synchrotron radiation.

KW - Bacterial Proteins/chemistry

KW - Carrier Proteins/chemistry

KW - Crystallization

KW - Polymerase Chain Reaction

KW - Recombinant Proteins/chemistry

KW - Streptococcus pneumoniae/chemistry

KW - Synchrotrons

KW - X-Ray Diffraction

U2 - 10.1107/S1744309107035865

DO - 10.1107/S1744309107035865

M3 - Journal article

C2 - 17768343

SN - 2053-230X

VL - 63

SP - 742

EP - 745

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt 9

ER -

Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae

Abstract

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