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11 citations found for Bingman, C.

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The crystal structure of the 18 kDa At3g22680 gene product from A. thaliana was determined at 1.6 Å resolution. At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformational space.

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The crystal structure of the 37.2 kDa At3g21360 gene product from A. thaliana was determined at 2.4 Å resolution. The structure establishes that this protein binds a metal ion and is a member of a clavaminate synthase-like superfamily in A. thaliana.

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The crystal structure of the 40.8 kDa At2g17340 protein from A. thaliana was determined at 1.7 Å resolution. The structure provides the first insight into the structural organization of the Pfam01937.11 family and establishes that the proteins of this family coordinate a metal in its putative active site.

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The crystal structure of the 27.5 kDa BLES03 protein was determined at 2.5 Å resolution. Despite having an undetectable sequence relationship, the structure adopts a fold similar to that of eukaryotic initiation factor 4E with minor variations.

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The crystal structure of the 28.3 kDa At4g34215 protein was determined at 1.6 Å resolution. The structure reveals a variation of the active site involved in the formation of an oxyanion hole that has not previously been described in the SGNH-hydrolase superfamily of enzymes.

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Adenosine 5′-monophosphate deaminase from A. thaliana has been crystallized in complex with coformycin 5′-phosphate. Diffraction data have been collected to 3.34 Å resolution.

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The crystal structure of AtETHE1 has been solved to a resolution of 1.48 Å. The structure has been analyzed and comparison is made to previously published structures of glyoxalase II enzymes.

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The crystal structure of T4moC from the toluene 4-monooxygenase of P. mendocina KR1 has been determined at a resolution of 1.48 Å. Structural analysis and comparison of T4moC with other structurally characterized Rieske-type ferredoxins is reported.


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The hexagonal crystal form of the octamer d(GTGTACAC), grown in the presence of spermine, has unit-cell dimensions a = b = 32.18 and c = 78.51 Å, space group P6122, with one DNA strand in the asymmetric unit. The structure has been refined starting with the earlier lower resolution model and using high-resolution 1.4 Å data collected on a Siemens-Xentronics area detector at 258 K. There were 4365 unique reflections greater than 2σ(F) in the resolution range 5–1.4 Å. The model was refitted into 3Fo − 2Fc. Sim-weighted omit maps and difference maps were used to locate water molecules. The final model with 161 DNA atoms and 37 water molecules gave an R factor of 19.8%. Crystals of the same octamer were also grown in the presence of spermidine instead of spermine, and refinement using nominal 1.45 Å resolution data, 3292 unique reflections, final R = 19.1%, gave virtually identical DNA parameters. No bound spermine or spermidine was detected in either of these structure analyses. The electron density was clear for the DNA and showed holes in the center of the six-membered rings of bases, and also in the center of some of the sugar rings. The high-resolution structure has provided more precise DNA parameters and confirmed the features observed in the earlier 2 Å study including the packing-induced distortion in the A7 (A15) sugar pucker from C(3′)-endo and C(2′)-endo. This change causes the end base pairs to bend away from the helix axis while the rest of the duplex is nearly linear. The hydration patterns in the deep and shallow grooves have been characterized. Chains of water molecules were found, but no rings. The familiar intermolecular contact region between the end base pair and the minor groove of a symmetry-related duplex, involving four residues on one strand and two on the other, has been analyzed. One of these interactions is a hydrogen bond.

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