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The crystal structure of the anti-diabetic drug target mitoNEET obtained from a GFP fusion construct (1.4 Å resolution, R factor = 20.2%) shows that the CDGSH 2Fe–2S binding domains are superimposable with previously determined non-fused constructs. However, there is considerable flexibility in the position of the outer mitochondrial tethering arms resulting in two different...
In the presence of Mn2+, a new crystal form of an echinomycin–d(ACGTACGT) complex is found which shows mixed base pairing next to the bis-intercalation site.
The crystal structure of the R482W mutant of the C-terminal domain of lamin A/C, which is responsible for familial partial lipodystrophy, has been determined at 1.5 Å resolution. A completely novel aggregation state of the mutated protein may be responsible for the changes in biological activity.
The structure of ribonuclease A in complex with uridine 5′-phosphate and uridine 5′-diphosphate has been determined at 1.4 Å resolution in order to facilitate the rational design of selective and potent inhibitors.
The S. agalactiae bifunctional ligase for glutathione synthesis has been crystallized. Native data were collected to 2.8 Å resolution.
Purification, crystallization and preliminary X-ray analysis of haemoglobin from ostrich (Struthio camelus) has been carried out under 293 K temperature conditions. The ostrich is a large flightless bird which contains inositol tetrakisphosphate in erythrocytes and its whole blood oxygen affinity is higher. Efforts have been made to explore the structure–function relationship of ostrich...
The N-terminal domain of FeoB from Methanococcus jannaschii was overproduced, purified to homogeneity and crystallized in the presence of GTP and magnesium.
The tetramerization domain of human Kv1.3 was cloned, expressed, purified and crystallized. The crystals belonged to space group I4 and diffracted to 1.2 Å resolution using synchrotron radiation.
An antibody–antigen complex consisting of a single-chain variable fragment of the potential therapeutic antibody chA21 and an N-terminal fragment (residues 1–192) of the human ErbB2 extracellular domain was expressed, purified and crystallized. X-ray diffraction data were collected to 2.45 Å resolution.
Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from A. salmonicida subsp. achromogenes, are reported.
The expression, purification and crystallization of a glycerol dehydrogenase from S. typhimurium is decribed. The crystals diffracted to 3.5 Å resolution.
Recombinant V. cholerae EpsH has been expressed, purified and crystallized. The crystals diffracted to 1.71 Å resolution.
Neutralizing Fab fragments of the HIV-2-binding murine antibody 7C8 were generated after purification from hybridoma cell-culture supernatant. Crystallization conditions were determined and diffraction data were collected to 2.7 Å resolution.
In order to study the structure and function of B. subtilis glycinamide ribonucleotide transformylase, the purN gene was amplified, cloned into an expression vector and expressed in soluble form in Escherichia coli. The protein was purified to homogeneity and crystals suitable for X-ray data collection were obtained.
The C-terminal domain of the S. gordonii surface protein SspB has been expressed, purified and crystallized. Diffraction data have been collected to 2.1 Å resolution.
The purification, crystallization and preliminary X-ray crystallographic analyses of the AAV9 viral capsid are reported.
The regulatory domain of response regulator YycF from an essential two-component signal transduction system has been crystallized and X-ray data have been collected at 1.95 Å resolution.
This manuscript describes the overexpression, purification and crystallization of human SOUL protein (hSOUL). hSOUL is a 23 kDa haem-binding protein that was first identified as the PP23 protein isolated from human full-term placenta.
The response regulator DesR from S. pneumoniae was cloned, expressed, purified and crystallized. A complete data set was collected to 1.7 Å resolution.
Diifraction data have been collected for the apo form of the orange protein from D. gigas to 2.25 Å resolution in-house and to beyond 2.0 Å resolution at ESRF, Grenoble. The crystals belonged to a trigonal space group, with unit-cell parameters a = 43, b = 43, c = 106 Å.
The enzyme phosphoglucosamine mutase from B. anthracis participates in the peptidoglycan-biosynthetic pathway. The expression, purification and crystallization of this enzyme are described; diffraction data have been collected to 2.7 Å resolution.
A 21 kDa Kunitz-type proteinase inhibitor was purified from tamarind (T. indica) seeds, crystallized and characterized by X-ray diffraction.
A fragment of the ADAMTS13 ancillary domains (ADAMTS13-DTCS) has been expressed, purified and crystallized and the crystals have been characterized by X-ray diffraction.
This article describes how CusB from E. coli was overexpressed and the recombinant protein purified using Ni–NTA affinity, Q anion-exchange and gel-filtration chromatography, and how the purified CusB protein was crystallized using the vapour-diffusion method.