Remarks about protein structure precision

Full-matrix least-squares is used to examine protein precision, both theoretically and by examples, for unrestrained and restrained refinements. Old and new approximate methods are compared critically.

Structure of the side-by-side binding of distamycin to d(GTATATAC)₂

The crystal structure of distamycin A binding side-by-side to the minor groove of d(GTATATAC)₂ has been determined.

Structure of de­thiobiotin synthetase at 0.97 Å resolution

The crystal structure of dethiobiotin synthetase has been refined to 0.97 Å resolution. A detailed analysis of the structure is presented.

Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 Å resolution

Crystals of a complex of R. miehei aspartic proteinase (RMP) with pepstatin A grew in the space group P2₁2₁2₁ and are isomorphous to the native RMP crystals. The structure was solved by molecular replacement.

Determination of the structure of selenome­thionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion

The MAD crystal structure of selenomethionine-labelled hydroxymethylbilane synthase, refined at 2.4 Å, is reported with the enzymic cofactor in its active reduced form and spherical density is seen to be consistent with there being a water molecule ideally placed for the final step of the catalytic reaction. As well as showing the effectiveness of the Daresbury SRS Station 9.5 for MAD protein crystallography, this work also establishes the credentials of the CCD for MAD data collection at ESRF Station BM14.

Mosaic spread characterization of microgravity-grown tetragonal lysozyme single crystals

Diffraction data from tetragonal lysozyme crystals grown in microgravity show very small values for mosaic spread (although comparable to those for good quality crystals grown on earth) as well as heterogeneity and anisotropy of the mosaic spread.

In-situ measurement of rocking curves during lysozyme crystal growth

An experimental set-up for in-situ diffraction experiments during protein crystal growth has been designed and used to assess the time evolution and spatial distribution of mosaic spread during crystal growth and its relation to growth kinetics.

An accurate numerical model for calculating the equilibration rate of a hanging-drop experiment

A numerical model of the equilibration of a hanging-drop experiment is described. The results of the calculations are compared to available experimental data, and the factors that influence the equilibration rate are discussed.

Crystallization and X-ray diffraction data of a tRNA^Sec acceptor-stem helix

The acceptor stem of the U6A suppressor tRNA^Sec carries determinants for the binding of the specific elongation factor SELB. The eight-base-pair RNA duplex was crystallized, and X-ray diffraction data were recorded.

Crystallization and preliminary X-ray diffraction studies of perchloric acid soluble protein (PSP) from rat liver

Perchloric acid soluble protein – a translational inhibitor – has been crystallized in space group P2₁3. Native diffraction data were collected to 1.8 Å resolution and data for platinum and xenon derivatives to 2.9 and 2.8 Å, respectively.

Crystallization and preliminary X-ray analysis of human muscle creatine kinase

Human muscle creatine kinase has been crystallized. The crystals are in space group or with and  Å and two subunits in the asymmetric unit.

Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A

Crystals of both the effector and regulatory domains of Spo0A from Bacillus stearothermophilus have been grown.

Cloning, crystallization and preliminary X-ray analysis of a nucleotide-di­phospho-sugar transferase spsA from Bacillus subtilis

A nucleotide-diphospho-sugar transferase involved in bacterial spore synthesis has been cloned, overexpressed and crystallized.

Cloning, overexpression, crystallization and preliminary X-ray analysis of a family 1 β-glucosidase from Streptomyces

-Glucosidase from Streptomyces has been crystallized in the trypsinized form with the use of synchrotron radiation. The crystals provide high-resolution diffraction (1.69 Å) and good data completeness.

Crystallization and preliminary X-ray analysis of plastocyanin from cyanobacterium Synechococcus sp. PCC 7942

Plastocyanin from Synechococcus sp. PCC7942 has been crystallized in two forms. Data have been obtained using Cu Kα and synchrotron radiation and molecular-replacement calculations performed.

Crystallization and preliminary X-ray diffraction studies of the lipopolysaccharide core biosynthetic enzyme ADP-L-glycero-D-mannoheptose 6-epimerase from Escherichia coli K-12

ADP-L-glycero-D-mannoheptose 6-epimerase is a lipopolysaccharide (LPS) core biosynthetic enzyme that catalyzes the interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. Three different crystal forms have been obtained one suitable for X-ray analysis.

Crystallization and preliminary X-ray analysis of the Rhodobacter capsulatus magnesium chelatase BchI subunit

The Bchl protein is one of three subunits of the magnesium chelatase, the enzyme which catalyses the first committed step in chlorophyll and bacteriochlorophyll biosynthesis. Crystals of heterologously expressed R. capsulatus Bchl belong to space group P6₃ with unit-cell dimensions a = b = 90.6, c = 84.1 Å and diffracted to 2.1 Å resolution.

Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain

A novel, highly thermostable phytase from B. amyloliquefaciens has been crystallized. Crystals diffracted to higher than 2.0 Å ­resolution.

Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amido­hydrolase from Agrobacterium radiobacter

N-carbamyl-D-amino-acid amidohydrolase from A. radiobacter has been expressed in E. coli JM109 and crystallized by vapour diffusion. Crystals diffract to 2.8 Å and are in space group P2₁ with cell dimensions a = 69.8, b = 67.9 and c = 137.8 Å and β = 96.4°.

Crystallization and preliminary X-ray analysis of tryparedoxin I from Crithidia fasciculata

Tryparedoxin I from C. fasciculata has been crystallized from PEG 4000 at pH 8.7. The crystals belong to the orthorhombic space group P2₁2₁2₁ and diffract to at least 1.7 Å.

Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly–Ser peptide bond hydrolysis

DmpA, an L-aminopeptidase from Ochrobactrum anthropi belonging to the Ntn hydrolase family, has been crystallized. Initial screening for heavy-atom derivatives has led to a well substituted Hg derivative and the structure determination by the MIR method is well under way.

Crystallization and preliminary X-ray diffraction studies of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis

Crystallization and preliminary X-ray analysis of the pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon T. litoralis.

Crystallization and preliminary X-ray diffraction studies of a DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8

A DNA excision repair enzyme, UvrB, from T. thermophilus HB8 has been crystallized. The crystals belong to space group P3₁21 or P3₂21 and diffracted X-rays to better than 2.9 Å resolution.

Purification, crystallization and preliminary structural studies of dTDP-6-de­oxy-D-xylo-4-hexulose 3,5-epimerase (RmlC), the third enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar Typhimurium

The synthesis of rhamnose is a potential therapeutic target in many bacteria. The preliminary structural study on RmlC, a key enzyme in the synthesis, is described.

A fully functional deletion staphylokinase derivative crystallizes in two non-isomorphous monoclinic modifications

Crystals suitable for structural investigation have been prepared from Δ10Sak, a fully functional staphylokinase derivative which lacks the first ten amino acids.

Preliminary characterization by X-ray diffraction and Raman spectroscopy of a crystalline complex of Bacillus stearothermophilus initiation factor 2 C-domain and fMet-tRNA^fMet

A complex of the C-terminal domain of B. stearothermophilus initiation factor 2 with fMet-tRNA^fMet has been crystallized. Raman spectroscopy proves the presence of both IF2-C and initiator tRNA in the crystals.

Separation and crystallization of T = 3 and T = 4 icosahedral complexes of the hepatitis B virus core protein

Recombinant-derived nucleocapsid of human hepatitis B virus formed a mixture of T = 3 and T = 4 icosahedral particles consisting of 90 and 120 dimers, respectively. The capsids were resolved by sucrose density centrifugation and crystallized; crystals of the T = 4 particles diffracted to 4 Å resolution and the T = 3 particles to 8 Å resolution.

Production of crystals of human aldose reductase with very high resolution diffraction

Crystals of aldose reductase, and enzyme involved in diabetes complications, diffract to 1.1 Å resolution at 103 K. Seleno-substituted crystals are also reported.

Portable xenon pressure chamber