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 Citations (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.

Original language	English
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	63
Issue number	Pt 9
Pages (from-to)	742-5
Number of pages	4
ISSN	2053-230X
DOIs	https://doi.org/10.1107/S1744309107035865
Publication status	Published - 1 Sept 2007

Keywords

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

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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.
In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 63, No. Pt 9, 01.09.2007, p. 742-5.

Research output: Contribution to journal › Journal article › Research › 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.",

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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

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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

Keywords

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