Preliminary crystallographic data on buffalo beta-lactoglobulin.

Lactoglobulin isolated from Italian buffalo milk has been crystallized in two different forms. Crystals of type I have been grown at pH 3.5 and belong to space group P6₃; the unit cell dimensions are $\text{a = b = 67}\text{A}\text{?}\text{, c = 142}\text{A}\text{?}$, and accordingly the asymmetric unit contains one dimer of molecular weight 36,000. Type II crystals, grown at pH 8.5, have only one monomer per asymmetric unit; the space group is P3₁21 (or enantiomorph) and the unit cell edges are: $\text{a = b = 54.4}\text{A}\text{?}\text{, c = 113.2}\text{A}\text{?}$. The crystals of the trigonal form show low radiation damage and are suitable for a structural investigation.     

Crystallographic data on a complete kappa-type human Bence-Jones protein.

A complete human κ-type Bence—Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence—Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P2₁2₁2₁ with cell dimensions $\text{a = 132.0}\text{A}\text{?}\text{, b = 93.3}\text{A}\text{?}\text{, and}\text{c = 42.3}\text{A}\text{?}$. The asymmetric unit consists of a dimer of molecular weight ~46,000.     

Preliminary crystallographic studies of triosephosphate isomerase from the blood parasite Trypanosoma brucei brucei

Crystals of triosephosphate isomerase (EC 5.3.1.1) from Trypanosoma brucei brucei have been grown. These crystals diffract to at least 2 Å, even after 60 hours of exposure to X-rays. The space group is P2₁2₁2₁, with cell dimensions $\text{a = 112.4}\text{A}\text{?}\text{, b = 97.8}\text{A}\text{?}\text{, c = 48.0}\text{A}\text{?}$. There is one dimer per asymmetric unit.     

Superoxide dismutase from Bacillus stearothermophilus: Crystallization and preliminary X-ray diffraction studies

Superoxide dismutase from Bacillus stearothermophilus is a dimeric manganese-containing enzyme with a molecular weight of 40,000. It has been crystallised in the monoclinic space group P2₁ with unit cell dimensions of $\text{a = 50}\text{A}\text{?}\text{, b = 70}\text{A}\text{?}\text{, c = 69}\text{A}\text{?}$ and β = 111 ° 10′. The asymmetric unit appears to be the dimer.     

Purification and preliminary crystallographic studies on azurin and cytochrome c' from Alcaligenes denitrificans and Alcaligenes sp. NCIB 11015.

Purification and crystallisation procedures are reported for azurin and cytochrome c′ from Alcaligenes denitrificans and Alcaligenes sp. NCIB 11015. The azurin crystals from A. denitrificans are suitable for high-resolution X-ray structure analysis. They are orthorhombic, space group C222₁ (with marked tetragonal pseudo-symmetry), cell dimensions $\text{a = 75.0}\text{A}\text{?}\text{, b = 74.1}\text{A}\text{?}\text{, c = 99.5}\text{A}\text{?}$, with two molecules per asymmetric unit. The cytochrome c′ crystals from both species are hexagonal, space group P6₁22 (or P6₅22), cell dimensions $\text{a = b = 54.7}\text{A}\text{?}\text{, c ~ 185}\text{A}\text{?}$, γ = 120 °, with one subunit (molecular weight 14,000) in the asymmetric unit.     

Crystallographic analysis of the phytoagglutinin from Abrus precatorius by X-ray diffraction and electron microscopy

The lectin from the seeds of Abrus precatorius has been crystallized and the crystals subjected to study by X-ray diffraction and electron microscopy. Three closely related crystal forms were obtained, of orthorhombic space group P2₁2₁2₁ with $\text{a = 138}\text{A}\text{?}$, $\text{b = 142}\text{A}\text{?}$, and $\text{c = 173}\text{A}\text{?}$, of tetragonal space group P4₁2₁2 with $\text{a = b = 136}\text{A}\text{?}$, $\text{c = 176}\text{A}\text{?}$, and a twinned intermediate of the first two. From electron microscopy and two-dimensional spatial filtering of electron micrographs of the crystals, the molecule appears to consist of four similar domains grouped in a roughly planar diamond-shaped arrangement having a local intramolecular dyad axis. The average diameter of the Abrus lectin molecule is 50 to 60 Å and the individual domains appear to have a diameter of about 25 Å.     

Crystallization of cow α-lactalbumin

Three new crystal forms of cow α-lactalbumin are described. A trigonal form in space group P3₁21 or P3₂21 has unit cell dimensions: $\text{a = b = 57.4}\text{A}\text{?}\text{, c = 75.0}\text{A}\text{?}$. A hexagonal form in space group P622 has unit cell dimensions: $\text{a = b = 94.0}\text{A}\text{?}\text{, c = 67.1}\text{A}\text{?}$. A second trigonal form grown in the presence of calcium ions belongs to space group P321 with unit cell dimensions: $\text{a = b = 93.7}\text{A}\text{?}\text{, c = 66.9}\text{A}\text{?}$. The significance of these new crystal forms to the structure determination of cow α-laetalbumin is discussed.     

Crystallization of and preliminary X-ray diffraction data for TET-repressor and the TET-repressor-tetracycline complex

The TET-repressor encoded by the transposon Tn10 has been crystallized along with the repressor-tetracycline complex. Both crystals belong to the space group P4₃2₁2 (or P4₁2₁2) with cell dimensions $\text{a = b = 74.3(1)}\text{A}\text{?}\text{, c = 94.2(2)}\text{A}\text{?}\text{and}\text{a = b = 73.3(1)}\text{A}\text{?}\text{, c = 94.6(2)}\text{A}\text{?}$ for the free and complexed repressor, respectively. There is one molecule of molecular weight 23,000 per asymmetric unit, and the biologically active dimer therefore consists of two identically formed subunits which are related by a crystallographic 2-fold axis. This isomorphism of TET-repressor and its tetracycline complex suggests that only minor, subtle changes in structure trigger binding to or release of the operator. The crystals of the native protein permit X-ray data collection to 3.2 Å and those of the complexed repressor to 2.8 Å.     

X-ray diffraction analysis of crystals of bovine platelet factor 4

Bovine platelet factor 4 has been crystallized by “vapor dilution” in space group P2₁2₁2₁, $\text{a = 63.7}\text{A}\text{?}\text{, b = 66.7}\text{A}\text{?}\text{, c = 80.5}\text{A}\text{?}$, with four molecules, each 9505 M_r, in the asymmetric unit. The crystals diffract X-rays to better than 2.8 Å resolution.     

Crystallization of alfalfa mosaic virus coat protein as a T = 1 aggregate

Reassembled alfalfa mosaic virus coat protein was partially digested with trypsin to remove the first 26 amino acids (Bol et al., 1974). These particles are empty icosahedral protein shells built with 60 alfalfa mosaic virus protein subunits. This aggregate has been crystallized in two different crystal forms, one of which diffracts X-rays to at least 3.4 Å resolution. The type I crystals (space group $\text{P6}{}_3\text{, a = 200}\text{A}\text{?}\text{, c = 314}\text{A}\text{?}$) contain two particles per cell separated by 195 Å with each sitting on a 3-fold axis. The type II crystals contain three particles per cell in space group P3₁or P3₂ ($\text{a = 201}\text{A}\text{?}\text{, c = 485}\text{A}\text{?}$). Other T = 1 viral particles have very similar diameters.     

Crystallographic study of the iron-sulfur flavoprotein trimethylamine dehydrogenase from the bacterium W3A1

Large single crystals of trimethylamine dehydrogenase, containing both [4Fe-4S]²⁺ centers and covalently bound FMN, have been prepared by the macro seeding technique. The crystals are monoclinic, space group P2₁ with cell parameters $\text{a = 147.63}\text{A}\text{?}\text{, b = 71.96}\text{A}\text{?}\text{, c = 83.66}\text{A}\text{?}\text{and}\text{β = 97.64 °}$, and diffract to at least 2.0 Å resolution. There is one dimer of approximately 166,000 M_m per asymmetric unit. A 5.0 Å resolution anomalous scattering difference Patterson has been computed which shows the presence and position of two [4Fe-4S]²⁺ centers in the asymmetric unit. A self-rotation function computed at 6.0 Å resolution indicates a non-crystallographic 2-fold axis relating the two subunits. These results show trimethylamine dehydrogenase to be composed of two identical or very similar subunits each containing one [4Fe-4S]²⁺ center.     

Preliminary crystallographic data on the human lambda III Bence Jones protein dimer Cle

A complete human λ Bence Jones protein dimer (Cle) has been isolated and crystallized. Protein Cle was characterized immunochemically and chemically as having a variable region amino acid sequence associated with light chains of the λ chain subgroup, λIII, and a constant region sequence characteristic of “non-Mcg” type λ chains. Bence Jones protein Cle contains two covalently bound intact monomers, each having a molecular weight of ~23,000. Crystals of Bence Jones protein Cle, obtained from ammonium sulfate solutions, diffract to 2.6 Å resolution and have the orthorhombic space group P2₁2₁2₁ with cell dimensions $\text{a = 113.0}\text{A}\text{?}\text{, b = 72.3}\text{A}\text{?}\text{,}\text{and}\text{c = 48.9}\text{A}\text{?}$. The asymmetric unit consists of a dimer with a molecular weight of ~ 46,000.     

Letter: Crystallization and preliminary x-ray investigation of bovine erythrocyte carbonic anhydrase

The major form of bovine erythrocyte carbonic anhydrase has been prepared by a new method in which the conventional chloroform-ethanol treatment is replaced by chromatography on DEAE-Sephadex. Single crystals, suitable for high resolution X-ray diffraction studies, have been obtained from enzyme prepared by this method. The space group is P6₁22. The unit cell contains 12 enzyme molecules and has the dimensions $\text{a = b = 68}\text{A}\text{?}$, $\text{c = 244}\text{A}\text{?}$.     

Crystallographic data for haemoglobin from the lanceolate fluke Dicrocoelium dendriticum

Two crystal modifications of the monomeric haemoglobin from the flatworm Dicrocoelium dendriticum have been obtained by vapour diffusion against buffered polyethylene glycol solutions. Both the triclinic and hexagonal crystals contain cyanomethaemoglobin. The triclinic modification, space group PI, $\text{a = 37.1}\text{A}\text{?}\text{, b = 39.9}\text{A}\text{?}\text{, c = 49.0}\text{A}\text{?}\text{, α = 88.8}\text{°}\text{, β = 76.8}\text{°}\text{, γ = 64.6}\text{°}$, with two molecules, M_r = 16,750 each, per unit cell, has been selected for a detailed crystallographic study.     

Crystallization of belladonna mottle virus

Belladonna mottle virus belongs to the turnip yellows mosaic virus group of the small spherical plant viruses. It contains 180 protein subunits, which are arranged in a T = 3 icosahedral surface lattice. The top and bottom viral components crystallize isomorphously in hexagonal space group R3 ($\text{a = b = 296}\text{A}\text{?}\text{, c = 729}\text{A}\text{?}$). The unit cell contains three virus particles, while the crystallographic asymmetric unit consists of only one-third of a particle. X-ray diffraction data from the crystals extend to at least 3.8 Å resolution.     

Preliminary studies of crystals of poliovirus type I

Poliovirus contains 60 copies each of four coat protein subunits arranged on a T = 1 icosahedral surface. Crystals of the Mahoney and the Sabin strains of the type I serotype of polio have been obtained. Crystals of the Mahoney strain belong to the orthorhombic space group P2₁2₁2 with $\text{a = 324}\text{A}\text{?}\text{, b = 359}\text{A}\text{?}\text{, c = 381}\text{A}\text{?}$, contain $\text{1}\text{2}$ virus particle in the asymmetric unit, and diffract to at least 2.5 Å resolution. The crystals are apparently identical to those characterized by Finch & Klug (1959). Collection of three-dimensional X-ray diffraction data to 2.9 Å resolution is in progress.     

A preliminary crystallographic study of wheat germ agglutinin

Wheat germ agglutinin crystallizes in two monoclinic space groups, P2₁ and C2, under identical crystallization conditions. Unit cell dimensions are $\text{a = 73.8}\text{A}\text{?}\text{, b = 51.2}\text{A}\text{?}\text{, c = 90.8}\text{A}\text{?}\text{, γ = 90 °}$ for $\text{P2}{}_1\text{; a = 51.31}\text{A}\text{?}\text{, b = 73.35}\text{A}\text{?}\text{, c = 91.45}\text{A}\text{?}\text{, β = 97.75 °}$ for C2, both with eight subunit molecules in the unit cell. The C2 crystals were chosen as suitable for investigating the three-dimensional structure to high resolution, because of their smaller asymmetric unit (containing the dimer), and also because they display better diffraction patterns.     

Letter: Crystallographic data of an L-arabinose-binding protein from Escherichia coli

Single crystals of an l-arabinose-binding protein from Escherichia coli B/r suitable for a high-resolution structural analysis have been obtained. An X-ray examination of the orthorhombic crystals shows the space group is P2₁2₁2₁, with unit cell dimensions: $\text{a = 55.3}\text{A}\text{?}\text{, b = 71.4}\text{A}\text{?}\text{and}\text{c = 77.5}\text{A}\text{?}$. The asymmetric unit contains one protein molecule with a molecular weight of 38,000.     

Molecular and crystal structure of the regenerated form of (1→3)-α-d-glucan

The crystal structure of a regenerated form of (1→3)-α-d-glucan, obtained by solid state deacetylation of the triacetate derivative, has been determined by combined X-ray diffraction analysis and stereochemical model refinement. The structure crystallizes in an orthorhombic unit cell with parameters $\text{a = 16.46}\text{A}\text{?}\text{, b = 9.55}\text{A}\text{?}$ and c (fibre repeat)=8.44 Å, and space group P2₁2₁2₁. The chain conformation is nearly completely extended and is very close to a 2/1 helix, even though the dimer residue is the crystallographic repeat unit. An intramolecular O(2)  O(4)′ hydrogen bond stabilizes the conformation and extensive intermolecular hydrogen-bonding abilizes the packing. The resulting structure is sheet-like, with an alternating polarity of chain directions within the sheet. In its sheet-like character, extensive hydrogen-bonding, and insolubility in water, this polymorph of (1→3)-α-d-glucan resembles regenerated cellulose. The reliability of the structure analysis is indicated by the X-ray residual R=0.206.     

Crystallization of cowpea chlorotic mottle virus

Cowpea chlorotic mottle virus belongs to the brome mosaic virus group of the small spherical plant viruses. It contains 180 protein subunits, which are arranged on a T = 3 icosahedral surface lattice. The virus crystallizes in orthorhombic space group P2₁2₁2 ($\text{a = 394}\text{A}\text{?}\text{, b = 382}\text{A}\text{?}\text{,}\text{and}\text{c = 397}\text{A}\text{?}$). The unit cell contains four virus particles, while the crystallographic asymmetric unit consists of one complete virion. X-ray diffraction data from the crystals extend to nearly 3.0 Å resolution.