issue contents
February 2014 issue
IYCr crystallization series
Approaches to automated and robot-assisted harvesting of protein crystals are critically reviewed. While no true turn-key solutions for automation of protein crystal harvesting are currently available, systems incorporating advanced robotics and micro-electromechanical systems represent exciting developments with the potential to revolutionize the way in which protein crystals are harvested.
structural communications
Polysaccharide deacetylases are bacterial enzymes that catalyze the deacetylation of acetylated membrane sugars on Gram-positive bacteria, allowing them to evade host immune systems. Here, the first X-ray crystal structure of BA0150, a putative polysaccharide deacetylase from B. anthracis, is reported to 2.0 Å resolution.
PDB reference: BA0150, 4m1b
The structure of the C-terminal domain of the CarD protein from M. tuberculosis is reported.
PDB reference: CarD83–161, 4kmc
Mass spectrometry was used to aid in the identification and structure determination of serendipitously purified glycerol dehydrogenase from the bacterial genus Serratia.
PDB reference: glycerol dehydrogenase, 4mca
Structures of the kinase domain of human tau-tubulin kinase 1 both without and with a bound inhibitor are reported.
crystallization communications
The SH2 domain of Grb7 has been crystallized in the apo form and in complex with a bicyclic peptide ligand. These structures will assist the development of potent Grb7 inhibitors as breast cancer therapeutics.
Crystals of glutathione transferase zeta 1 were grown and shown to diffract X-rays to 3.1 Å resolution. They belonged to space group P1, with unit-cell parameters a = 42.0, b = 49.6, c = 54.6 Å, α = 82.9, β = 69.9, γ = 73.4°.
MutT2, MSMEG_5148 from M. smegmatis, has been crystallized and the crystals have been characterized using X-ray diffraction.
Est24 from S. meliloti was crystallized in the monoclinic space group C2 and diffraction data were collected to 1.45 Å resolution.
The molecular chaperone CfaA plays a critical role in the bioassembly of the surface-adhesive CFA/I fimbriae of enterotoxigenic E. coli. Purified CfaA was crystallized and the phase solution was determined by the multiple isomorphous replacement coupled with anomalous scattering method.
Flagellin from P. aeruginosa was expressed, purified and crystallized. X-ray diffraction data were collected from a flagellin crystal to a resolution of 2.15 Å.
UDP-glucose:tetrahydrobiopterin α-glucosyltransferase from Synechococcus sp. PCC 7942 was purified and crystallized, and MAD diffraction data were collected to a maximum resolution of 1.99 Å.
The cloning, expression, purification and crystallization of human DNA primase are reported. Two crystal forms were obtained.
The crystallization of the N-acetyltransferase SAV0826 from S. aureus is reported.
An aromatic acid decarboxylase from C. psychrerythraea strain 34H was expressed, purified and crystallized. Furthermore, preliminary X-ray crystallographic analysis of the FMN-bound and FMN-free forms was performed at resolutions of 2.0 and 1.76 Å, respectively.
Dipeptidyl aminopeptidase BII from P. mexicana WO24 was crystallized. X-ray diffraction data were collected to 2.3 Å resolution.
A GH1 6-phospho-β-galactosidase from G. stearothermophilus T1 (Gan1D) has been purified and crystallized in the triclinic space group P1. A full diffraction data set has been measured for the wild-type enzyme to a maximal resolution of 1.33 Å to be further used for a detailed three-dimensional structural analysis of the protein.
The crystallization of the recombinant catalytic domain of the human membrane type 1 matrix metalloproteinase is described. The crystals diffracted to 2.24 Å resolution.
LePRK1 is a receptor-like kinase (RLK) involved in successful fertilization in L. esculentum (tomato). The extracellular leucine-rich repeat (LRR) domain of LePRK1 was crystallized and X-ray diffraction data were collected to a resolution of 2.75 Å.
LePRK2 is a member of the large receptor-like kinase (RLK) family and is expressed specifically in mature pollen and pollen tubes in L. esculentum. The extracellular leucine-rich repeat (LRR) domain of LePRK2 was crystallized and X-ray diffraction data were collected to a resolution of 2.50 Å.
The crystallization of a PaaI-like thioesterase from S. aureus is reported.
Full-length human RIG-I has been expressed in E. coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 2.85 Å.
D. discoideum DdDyP was purified and crystallized. The crystals belonged to space group P41212 and diffracted to 1.65 Å resolution.
The homing endonuclease I-CvuI from C. vulgaris has been expressed, purified and crystallized in complex with its target DNA. Preliminary X-ray diffraction analysis is reported.
The C-type lectin domain of the spicule matrix protein SM50 from S. purpuratus was purified and crystallized as a fusion protein with SUMO.
Open access
Polyphenol oxidase 4 (PPO4) from the natural source A. bisporus was crystallized in its latent precursor form (pro-tyrosinase; Ser2–Thr565) using the 6-tungstotellurate(VI) salt Na6[TeW6O24]·22H2O as a crystallization additive.
The A. terreus endo-β-1,4-glucanase was expressed in E. coli, purified and crystallized. A native X-ray diffraction data set was collected to 1.85 Å resolution.