issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2015 issue

Highlighted illustration

Cover illustration: Crystal structure of anti-influenza apo CH65 Fab (Lee et al., p. 145). Overall Fab structure is shown with the heavy chain and light chain coloured blue and green, respectively. The heavy-chain CDR loop 3 is shown as thick tubes. The variable and constant Ig domains for each antibody chain are labelled.

IYCr crystallization series


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Fluorescence, whether intrinsic or by using trace fluorescent labeling, can be a powerful aid in macromolecule crystallization. Its use in screening for crystals is discussed here.

research communications



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The P. barcinonensis xylanase 10C N-terminal domain, containing the CBM22-1–CBM22-2 tandem, was overexpressed, purified and crystallized, and its preliminary X-ray diffraction analysis is reported at 2.43 Å resolution.

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HutX from V. cholerae was expressed, purified and crystallized. The crystals were of sufficient quality to collect high-resolution data sets and carry out a preliminary X-ray crystallographic analysis.

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The crystal structure of anti-influenza antibody CH65 at 1.70 Å resolution reveals that the affinity-matured antibody evolved to preconfigure the antibody loops to increase binding affinity to the hemagglutinin.

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VioD, a hydroxylase in the violacein-biosynthesis pathway, was crystallized and a complete 1.7 Å resolution data set was collected. The crystal belonged to space group P31, with unit-cell parameters a = b = 90.0, c = 94.5 Å, α = β = 90, γ = 120°.

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Tomato β-galactosidase 4 has been expressed in P. pastoris, purified and crystallized. Diffraction data have been collected to a resolution of 1.65 Å.

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The role of surface flexibility and molecular shape in protein crystallization is investigated.


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RGA5-A_S, the effector-interaction domain of the resistance protein RGA5-A, was expressed, purified and crystallized, yielding crystals that diffracted to 2.43 Å resolution.

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The crystal structure of the TPR domain of LGN in complex with the LGN binding region of Frmpd4/Preso1 is presented at 1.5–Å resolution. Comparison with structures of LGN complexed with its other partners has identified the consensus sequence motif (E/Q)XEX4–5(E/D/Q)X1–2(K/R)X0–1(V/I) as the common core LGN-binding region.

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A variant of human galectin-3 containing sections of the N-terminal domain has been crystallized for the first time. The crystals belonged to the orthorhombic space group P212121 and diffracted to 3.3 Å resolution.

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The M. smegmatis gene Msmeg_0515 encoding the AgaE protein has been cloned, expressed in E. coli and purified. Crystals of AgaE have been grown that diffracted to beyond 1.5 Å resolution and belonged to space group P212121 with a single AgaE polypeptide in the asymmetric unit.

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The E. coli ZapD protein was expressed in E. coli, purified and crystallized using lithium sulfate as a precipitant. X-ray diffraction data were collected to 2.95 Å resolution.

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The crystal structure of a substrate-trapping mutant of human dual-specificity phosphatase 22 (DUSP22) in complex with the small molecule substrate 4-nitrophenyl phosphate was determined at 1.34 Å resolution.

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Dipeptidyl peptidase 11 from P. gingivalis (PgDPP11) was crystallized. X-ray diffraction data were collected to 1.82 Å resolution.

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A periplasmic sensory domain of the C. jejuni chemoreceptor for multiple ligands (CcmL) has been purified and co-crystallized with isoleucine by the hanging-drop vapour-diffusion method. A diffraction data set has been collected to 1.3 Å resolution.


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SM80.1, a 7S vicilin from S. melongena, was identified, purified and crystallized. The crystals belonged to space group P6322 and diffracted to 2.21 Å resolution.

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The HigA2 antitoxin and the HigBA2 toxin–antitoxin complex from V. cholerae were crystallized in complex with their operator box.

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In this study, the recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of Haemophilus influenzae BamD and BamCD complex are reported.

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The crystallization and preliminary X-ray diffraction analysis of a putative carbon–carbon bond hydrolase from M. abscessus 103 are reported.

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A soluble variant of the monoglyceride lipase Yju3p was successfully expressed, purified and crystallized. Diffraction data were collected to 2.4 Å resolution.
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