Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
J Synchrotron Radiat ; 15(Pt 2): 140-3, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18296779

ABSTRACT

A scanning dynamically focusing sagittal X-ray monochromator accepting 3 mrad x 0.1 mrad from a 6 T wiggler has been designed for XAFS measurements. In the energy range 4.1-12.4 keV, the slope error of the second cylindrical crystal caused by anticlastic bending must be less than 1/5 of the Darwin width of the crystal or the photon flux will decrease drastically. Two methods to minimize the anticlastic bending are proposed. Thin crystals with stiffening ribs and thin crystals with an aspect ratio equal to the ;golden value' are evaluated by finite-element analysis and by long-trace-profiler characterization. Both approaches are satisfactory, but the ;golden value' approach is preferred in this case for the second crystal of the new monochromator not only because it is easy to manufacture but also because the surface is smoother than the ribbed crystal.

2.
Acta Crystallogr D Biol Crystallogr ; 59(Pt 6): 1038-42, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12777767

ABSTRACT

Atratoxin-b, a short-chain alpha-neurotoxin purified from Naja atra (mainland Chinese cobra) venom using a three-step chromatography procedure, has an apparent molecular mass of 6950 Da with an alkaline pI value (>9.5) and consists of one single polypeptide chain as estimated by MALDI-TOF mass spectrometry and SDS-PAGE. The protein is toxic to mice, with an in vitro LD(50) of about 0.18 mg kg(-1). Its N-terminal amino-acid sequence, LECHNQQSSQTPTIT, displays a very high homology to those of other alpha-neurotoxins. The overall three-dimensional structure of atratoxin-b is very similar to that of the homologous erabutoxin-a, as shown by the crystallographic molecular replacement and preliminary refinement results, with an R factor and R(free) of 27 and 29%, respectively. The microcrystal slowly grew to dimensions of approximate 0.1 x 0.1 x 0.15 mm over eight months using hanging-drop vapour-diffusion method. It gave a set of diffraction data to 1.56 A resolution using X-rays of wavelength 1.1516 A generated by the X-ray Diffraction and Scattering Station of beamline U7B at the National Synchrotron Radiation Laboratory (Hefei, China); this is the first example of the use of this beamline in protein crystallography. The crystals belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = 49.28, c = 44.80 A, corresponding to one molecule per asymmetric unit and a volume-to-mass ratio of 1.96 A(3) Da(-1).


Subject(s)
Elapid Venoms/chemistry , Neurotoxins/chemistry , Amino Acid Sequence , Animals , Crystallization , Electrophoresis, Polyacrylamide Gel , Hydrogen Bonding , Insect Proteins , Mice , Models, Molecular , Neurotoxins/isolation & purification , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , X-Ray Diffraction
SELECTION OF CITATIONS
SEARCH DETAIL
...