Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone

Biosynthesis and Export of Bacterial Lipopolysaccharides

(2014) Chris Whitfield et al.   Annual Review of Biochemistry

Crystallization of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34

(2014) Meritxell Granell et al.   Acta Crystallographica Section F-Structural Biology Communications

Developments in optics and performance at BL13-XALOC, the macromolecular crystallography beamline at the Alba Synchrotron

(2014) Jordi Juanhuix et al.   JOURNAL OF SYNCHROTRON RADIATION

How good are my data and what is the resolution?

(2013) Philip R. Evans et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre

(2013) Carmela Garcia-Doval et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components

(2013) Y. Zivanovic et al.   JOURNAL OF VIROLOGY

Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17

(2012) Carmela Garcia-Doval et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Prokaryote viruses studied by electron microscopy

(2012) H.-W. Ackermann et al.   ARCHIVES OF VIROLOGY

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

(2012) C. Garcia-Doval et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Bacteriophages and their Implications on Future Biotechnology: A Review

(2012) Irshad UL Haq et al.   Virology Journal

iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM

(2011) T. Geoff G. Battye et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

REFMAC5 for the refinement of macromolecular crystal structures

(2011) Garib N. Murshudov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Knitting and snipping: chaperones in β-helix folding

(2011) Eike C Schulz et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Experimental phasing withSHELXC/D/E: combining chain tracing with density modification

(2010) George M. Sheldrick   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

The K5 Lyase KflA Combines a Viral Tail Spike Structure with a Bacterial Polysaccharide Lyase Mechanism

(2010) James E. Thompson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal structure of an intramolecular chaperone mediating triple–β-helix folding

(2010) Eike C Schulz et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Dali server: conservation mapping in 3D

(2010) Liisa Holm et al.   NUCLEIC ACIDS RESEARCH

Structure of the bacteriophage T4 long tail fiber receptor-binding tip

(2010) S. G. Bartual et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Crystallographic Insights into the Autocatalytic Assembly Mechanism of a Bacteriophage Tail Spike

(2009) Ye Xiang et al.   MOLECULAR CELL

Two-chaperone assisted soluble expression and purification of the bacteriophage T4 long tail fibre protein gp37

(2009) Sergio Galan Bartual et al.   PROTEIN EXPRESSION AND PURIFICATION

Image processing for electron microscopy single-particle analysis using XMIPP

(2008) Sjors H W Scheres et al.   Nature Protocols