issue contents
February 2015 issue
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
Open access
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
The preliminary structural analysis of VSR in complex with the C-terminal sorting determinant of a seed storage protein is reported.
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.
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.
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.
PDB reference: apo CH65 Fab, 4wuk
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°.
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.
The role of surface flexibility and molecular shape in protein crystallization is investigated.
The ligand-binding properties of human adipocyte fatty-acid binding protein is crystallographically probed with a set of compounds structurally related to ibuprofen.
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.
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.
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.
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.
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.
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.
Dipeptidyl peptidase 11 from P. gingivalis (PgDPP11) was crystallized. X-ray diffraction data were collected to 1.82 Å resolution.
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.
The paper describes the purification, crystallization and preliminary structural analysis of ctCBM54.
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.
The HigA2 antitoxin and the HigBA2 toxin–antitoxin complex from V. cholerae were crystallized in complex with their operator box.
In this study, the recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of Haemophilus influenzae BamD and BamCD complex are reported.
The crystallization and preliminary X-ray diffraction analysis of a putative carbon–carbon bond hydrolase from M. abscessus 103 are reported.
Open access
A soluble variant of the monoglyceride lipase Yju3p was successfully expressed, purified and crystallized. Diffraction data were collected to 2.4 Å resolution.