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Native Diffraction Data (native + diffraction_data)

Distribution by Scientific Domains

Chemistry	100%

Selected Abstracts

Crystallization and preliminary X-ray characterization of a novel calcium-binding protein AtCBL2 from Arabidopsis thaliana

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2003
Masamichi Nagae
A new family of calcineurin B-like calcium-binding proteins has recently been identified in Arabidopsis thaliana. AtCBL2, a member of this family, has been crystallized in the presence of calcium ions using polyethylene glycol as a precipitant at 293,K. The crystals belong to space group C2221, with unit-cell parameters a = 83.9, b = 118.1, c = 49.1,Å. The asymmetric unit contains one molecule, with a VM of 2.36,Å3,Da,1 and a solvent content of 48%. Native diffraction data to 2.1,Å resolution have been collected using synchrotron radiation at SPring-8. [source]

Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp.

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2009
BSAR-
Alkaline phosphatases (APs) are widely distributed from microbes to humans and are involved in several important biological processes such as phosphate nutrition, signal transduction and pathogenesis. Alkaline phosphatases are also useful in various industrial applications and in recombinant DNA technology. A new AP enzyme from Sphingomonas sp. strain BSAR-1, termed PhoK, has been shown to be useful in uranium bioprecipitation. PhoK was expressed, purified and crystallized. The crystals belonged to space group P43212 or P41212, with unit-cell parameters a = b = 87.37, c = 168.16,Å, and contained one enzyme molecule in the asymmetric unit. Native diffraction data have been collected to 1.95,Å resolution at the ESRF. [source]

Purification, crystallization and preliminary X-ray crystallographic study of the l -fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2005
Jeyaraman Jeyakanthan
Fuculose phosphate aldolase catalyzes the reversible cleavage of l -fuculose-1-phosphate to dihydroxyacetone phosphate and l -lactaldehyde. The protein from Thermus thermophilus HB8 is a biological tetramer with a subunit molecular weight of 21,591,Da. Purified FucA has been crystallized using sitting-drop vapour-diffusion and microbatch techniques at 293,K. The crystals belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87,Å. The presence of a dimer of the enzyme in the asymmetric unit was estimated to give a Matthews coefficient (VM) of 2.7,Å3,Da,1 and a solvent content of 54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3,Å from zinc-containing crystals. Native diffraction data to 1.9,Å resolution have been collected using synchrotron radiation at SPring-8. [source]

DIBER: protein, DNA or both?

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2010
Grzegorz Chojnowski
The program DIBER (an acronym for DNA and FIBER) requires only native diffraction data to predict whether a crystal contains protein, B-form DNA or both. In standalone mode, the classification is based on the cube root of the reciprocal unit-cell volume and the largest local average of diffraction intensities at 3.4,Å resolution. In combined mode, the Phaser rotation-function score (for the 3.4,Å shell and a canonical B-DNA search model) is also taken into account. In standalone (combined) mode, DIBER classifies 87.4 ± 0.2% (90.2 ± 0.3%) of protein, 69.1 ± 0.3% (78.8 ± 0.3%) of protein,DNA and 92.7 ± 0.2% (90.0 ± 0.2%) of DNA crystals correctly. Reliable predictions with a correct classification rate above 80% are possible for 36.8 ± 1.0% (60.2 ± 0.4%) of the protein, 43.6 ± 0.5% (59.8 ± 0.3%) of the protein,DNA and 83.3 ± 0.3% (82.6 ± 0.4%) of the DNA structures. Surprisingly, selective use of the diffraction data in the 3.4,Å shell improves the overall success rate of the combined-mode classification. An open-source CCP4/CCP4i -compatible version of DIBER is available from the authors' website at http://www.iimcb.gov.pl/diber and is subject to the GNU Public License. [source]