|Home | About | Journals | Submit | Contact Us | Français|
The crystal structure of bovine pancreatic ribonuclease A in complex with uridine 5′-monophosphate was determined at 1.60 Å resolution. The uridine lies in the pyrimidine-specific binding site of the enzyme, with the phosphate group extended into the solvent without interacting with the protein.
The crystal structure of B. amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family.
The crystal structure of uracil-DNA N-glycosylase from Vibrio cholerae has been determined at 1.5 Å, and used for mapping temperature adaptation.
The structure of human diamine oxidase has been refined to 2.1 Å resolution in space group C2221.
A 1.9 Å resolution crystal structure of the isolated kinase domain from the α2 subunit of human AMPK, the first from a multicellular organism, is presented.
The crystal structure of an O-sulfated thiohydroximate inhibitor bound to S. alba myrosinase is reported.
The expression, purification and crystallization of the collagen-binding region of the E. rhusiopathiae surface protein RspB is described. The crystals diffracted to 2.2 Å resolution using synchrotron radiation.
In this study, d,d-heptose-1,7-bisphosphate phosphatase has been cloned, expressed, purified and crystallized.
Recombinant P. somniferum salutaridine reductase (SalR) was purified and crystallized with NADPH using the hanging-drop vapor-diffusion method. Crystals of the SalR–NADPH complex diffracted X-rays to a resolution of 1.9 Å.
The antitoxin Phd from the phd/doc operon of bacteriophage P1 was crystallized in two distinct crystal forms.
The purification, crystallization and preliminary X-ray diffraction analysis of a surface-associated antigen from the major human hookworm N. americanus is presented.
The minor pilin FctB from S. pyogenes strain 90/306S was expressed in E. coli, purified and crystallized. The hexagonal FctB crystals diffracted to 2.9 Å resolution.
SAICAR synthetase from P. horikoshii OT3 has been cloned, expressed, purified and crystallized.
1,3-Propanediol dehydrogenase (Aq_1145) from A. aeolicus VF5 has been overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution.
Recombinant glycine decarboxylase from Synechocystis sp. PCC 6803 was expressed in E. coli and purified to homogeneity. Crystals were obtained that diffracted to 2.1 Å resolution using synchrotron radiation.
The production and crystallization of the human DEAD box polypeptide 5 are reported. A 2.7 Å native diffraction data set has been obtained.
Crystals of the Grb2 SH2 domain in complex with a phosphotyrosyl peptide corresponding to residues 921–930 of focal adhesion kinase (FAK) have been obtained using the sitting-drop vapour-diffusion technique. Data have been collected to 2.49 Å resolution.
In this study, the mature form of SPN48 was overexpressed in Escherichia coli and purified. The purified SPN48 protein was crystallized using 14% polyethylene glycol 8000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid pH 6.0 as the precipitant. The crystals diffracted X-rays to 2.1 Å resolution and were suitable for structure determination.
VSP1 from Arabidopsis thaliana was expressed in E. coli, purified and crystallized. X-ray diffraction data were collected to 1.9 Å resolution.
Psu, a unique 21 kDa protein from bacteriophage P4, is a non-essential capsid-decoration protein that inhibits Rho-dependent termination specifically and efficiently both in vivo and in vitro. Psu has been crystallized using PEG as precipitant and the crystals diffracted to 2.3 Å resolution.
E. cuniculi Iws1, which acts in eukaryotic transcription and mRNA processing and export, has been crystallized and data have been collected to 2.5 Å resolution.
The FAF1 UBX domain was crystallized. X-ray diffraction data were collected to 3.00 Å resolution and the crystals belonged to space group F4132.
Addendum to Hee et al. [Acta Cryst. (2009), F65, 422–425].