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R.m.s. Deviation (r.m.s. + deviation)

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Chemistry100%

Selected Abstracts

7-Methoxy-2,3-dioxo-1,4-dihydroquinoxalin-6-aminium chloride monohydrate

ACTA CRYSTALLOGRAPHICA SECTION C, Issue 1 2010
Jürgen Brüning
Single crystals of the title compound, C9H10N3O3+·Cl,·H2O, were obtained by recrystallization from hydrochloric acid. The cations stack along the crystallographic a direction. The 2,3-dioxo-1,4-dihydroquinoxaline group shows a significant deviation from planarity [r.m.s. deviation from the best plane = 0.063,(2),Å]. Hydrogen bonding links the cations, chloride anions and water molecules to form an extended three-dimensional architecture. [source]

Structural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargeting

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2010
Snezana Djordjevic
In a subset of patients with the hereditary kidney-stone disease primary hyperoxaluria type 1 (PH1), the liver-specific enzyme alanine:glyoxylate aminotransferase (AGT) is mistargeted from peroxisomes to mitochondria. This is a consequence of the combined presence of the common P11L polymorphism and a disease-specific G170R mutation. In this paper, the crystal structure of mutant human AGT containing the G170R replacement determined at a resolution of 2.6,Å is reported. The crystal structure of AGT consists of an intimate dimer in which an extended N-terminal segment of 21 amino acids from one subunit wraps as an elongated irregular coil around the outside of the crystallographic symmetry-related subunit. In addition to the N-terminal segment, the monomer structure contains a large domain of 261 amino acids and a small C-terminal domain of 110 amino acids. Comparison of the mutant AGT structure and that of wild-type normal AGT shows that the two structures are almost identical, with a backbone-atom r.m.s. deviation of 0.34,Å. However, evidence of significant local structural changes in the vicinity of the G170R mutation might be linked to the apparent decrease in protein stability. [source]

(Di- tert -butylmethylphosphane)(,2 -di- tert -butylphosphanylphosphinidene)(triphenylphosphane)platinum(0)

ACTA CRYSTALLOGRAPHICA SECTION C, Issue 1 2009
Antoni Konitz
The crystal structure of the title compound, [Pt(C8H18P2)(C9H21P)(C18H15P)] or [(Ph3P)(tBu2PMe)Pt(,2 - tBu2PP)], contains four molecules in the asymmetric unit with slightly different conformations. The P,P distances in the tBu2PP ligands are similar for all four molecules [2.0661,(13),2.0678,(13),Å] and indicate a multiple character of the P,P bond in the tBu2PP ligand. Molecules of the asymmetric unit can be assembled into a tetrahedron that fulfils the requirements for a rhombic disphenoid. The coordination of the Pt atom in all four molecules is square planar, with r.m.s. deviations from the PtP4 planes in the range 0.03,0.05,Å. All planes of the PtP4 groups are approximately parallel to the ab plane of the unit cell. The structure represents an unusual unsymmetrical platinum phosphinidene derivative. [source]

High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5,AMP

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 11 2001
Pascal Retailleau
Native data, anomalous data at three wavelengths and an independent peak-wavelength data set for SeMet-substituted protein have been collected from cryoprotected crystals of the TrpRS,adenylate product (TAM) complex to a resolution limit of 1.7,Å. Independent phase sets were developed using SHARP and improved by solvent flipping with SOLOMON using molecular envelopes derived from experimental ­densities for, respectively, peak-wavelength SAD data from four different crystals, MAD data and their M(S)IRAS ­combinations with native data. Hendrickson,Lattman phase-probability coefficients from each phase set were used in BUSTER to drive maximum-likelihood refinements of well defined parts of the previously refined room-temperature 2.9,Å structure. Maximum-entropy completion followed by manual rebuilding was then used to generate a model for the missing segments, bound ligand and solvent molecules. Surprisingly, peak-wavelength SAD experiments produced the smallest phase errors relative to the refined structures. Selenomethionylated models deviate from one another by 0.25,Å and from the native model by 0.38,Å, but all have r.m.s. deviations of ,1.0,Å from the 2.9,Å model. Difference Fourier calculations between amplitudes from the 300,K experiment and the new amplitudes at 100,K using 1.7,Å model phases show no significant structural changes arising from temperature variation or addition of cryoprotectant. The main differences between low- and high-resolution structures arise from correcting side-chain rotamers in the core of the protein as well as on the surface. These changes improve various structure-validation criteria. [source]