Error estimates in the determination of rigid body displacements in protein crystals

We report the estimation of random errors in the refinement of the rigid body displacements of the -helices of the enzyme 6-phosphogluconate dehydrogenase. Least-squares refinement of the TLS parameters of the helices has been carried out using X-ray reflection data of 2.1 Å resolution, resulting in anR-factor of 19.5%. Standard deviations were estimated from the normal matrix. The results show that the translational mean-square displacements of nearly all the helices are significant at this resolution. However the libration parameters are only significant when the helices have at least four turns. Screw-rotation tensor values cannot be determined at this resolution.     

Induced radioactivity of LDEF materials and structural components

We present an overview of the Long Duration Exposure Facility (LDEF) induced activation measurements. The LDEF, which was gravity-gradient stabilized, was exposed to the low Earth orbit (LEO) radiation environment over a 5.8 year period. Retrieved activation samples and structural components from the spacecraft were analyzed with low and ultra-low background HPGe gamma spectrometry at several national facilities. This allowed a very sensitive measurement of long-lived radionuclides produced by proton- and neutron-induced reactions in the time-dependent, non-isotropic LEO environment. A summary of major findings from this study is given that consists of directionally dependent activation, depth profiles, thermal neutron activation, and surface beryllium-7 deposition from the upper atmosphere. We also describe a database of these measurements that has been prepared for use in testing radiation environmental models and spacecraft design.     

A Product Formed from Glycylglycine in the Presence of Vanadate and Hydrogen Peroxide: The (Glycylde-N-hydroglycinato-kappa(3)N(2),N(N)(),O(1))oxoperoxovanadate(V) Anion

A crystalline glycylglycine complex of monoperoxovanadate has been obtained and its X-ray structure determined. The coordination is pentagonal bipyramidal with the peroxo group and a tridentate glycylglycine occupying the equatorial positions. The axial positions of the anion are occupied by the oxo ligand and by one oxygen of the peroxo group of the adjacent anion. The latter interaction establishes the seventh bond and produces a dimeric structure in the crystalline material. NMR studies of its dissolution in water combined with previously reported results from equilibrium measurements show that the dimer dissociates in water to the monomeric precursor. It is proposed that this monomer corresponds to the complex responsible for the inhibition of the vanadium-catalyzed decomposition of hydrogen peroxide by glycylglycine. Crystal structure of [NEt(4)][VO(O(2))(GlyGly)].1.58H(2)O: monoclinic, space group P2(1); Z = 4; a = 10.618(2) ?; b = 14.803(2) ?; c = 11.809(2) ?; beta = 101.37(2) degrees; V = 1819.7 ?(3); T = 198 K; R(F)() = 0.029 for 2664 data (I(o) >/= 2.5sigma(I(o))) and 431 variables.