Crystallographic data for lysozyme from the egg white of the Embden goose

Two crystal forms of lysozyme from the egg white of the embden goose (Anser anser) have been obtained, both of which are suitable for X-ray diffraction analysis. The monoclinic form has space group P2₁ with cell dimensions $\text{a = 38.3}\text{A}\text{?}\text{, b = 65.7}\text{A}\text{?}\text{, c = 45.2}\text{a}\text{?}$, β = 116 ° and the triclinic form (space group P1) has cell dimensions of $\text{a = 39.9}\text{A}\text{?}\text{, b = 42.2}\text{A}\text{?}\text{, c = 57.9}\text{A}\text{?}$ and α = 98.8 °, β = 102.5 °, γ = 90.5 °.     

Characterization of two crystal forms of neutrophil cationic protein NP2, a naturally occurring broad-spectrum antimicrobial agent from leukocytes

A hexagonal crystal form (P6₃22, $\text{a = b = 34.0}\text{A}\text{?}\text{, c = 113.5}\text{A}\text{?}$) and a monoclinic form (P2₁, $\text{a = 37.1}\text{A}\text{?}\text{, b = 32.2}\text{A}\text{?}\text{, c = 32.4}\text{A}\text{?}\text{, β = 110 °}$) of neutrophil cationic protein NP2, isolated from rabbit leukocytes, have been characterized. The monoclinic form, containing two promoters (M_r = 3844) per asymmetric unit, diffracts to at least 1.8 Å and is suitable for high-resolution structural studies.     

X-ray analysis of a progesterone-binding protein (uteroglobin): preliminary results

Uteroglobin, which is a progesterone-binding protein of the rabbit uterine secretion, has been crystallized and subjected to X-ray diffraction analysis. Two crystalline forms have been observed: a triclinic one ($\text{P1, Z = 2, a = 36.36 (4)}\text{A}\text{?}\text{, b = 37.40 (4)}\text{A}\text{?}\text{, c = 53.28 (4)}\text{A}\text{?}\text{, α = 104.6 (1) °, β = 97.0 (1) °, γ = 111.3(1) °}$); and an orthorhombic one for which the cell is C-centred with $\text{a = 50.86 (5)}\text{A}\text{?}\text{, b = 52.22 (5)}\text{A}\text{?}\text{, c = 47.28 (5)}\text{A}\text{?}$, space group C222₁, Z = 4. Three isomorphous derivatives have been obtained. The crystals appear suitable for detailed study of the three-dimensional structure of the protein.     

Preliminary crystallographic study of macromomycin: The apoprotein of the antitumor antibiotic auromomycin

Macromomycin (M_r 12,000) is the apoprotein of the antitumor drug auromomycin, which inhibits DNA synthesis by causing single-strand breaks in DNA. Two orthorhombic crystal forms of macromomycin have been observed. The platelike crystals of one form belong to space group P2₁2₁2₁, with cell dimensions $\text{a = 48·92}\text{A}\text{?}\text{, b = 54·71}\text{A}\text{?}\text{, c = 103·31}\text{A}\text{?}\text{, Z = 8}$. The crystals of the second form are needle-shaped, and belong to space group P2₁2₁2, with cell dimensions $\text{a = 46·1}\text{A}\text{?}\text{, b = 54·4}\text{A}\text{?}\text{, c = 41·2}\text{A}\text{?}\text{, Z = 4}$. At this point in time, the platelike crystals appear the most suitable for continued crystallographic studies.     

Preliminary X-ray data for the ribose binding protein from Salmonella typhimurium

Crystals of the periplasmic ribose binding protein of Salmonella typhimurium have been subjected to X-ray analysis. The crystals grow as rectangular parallelopipeds with the symmetry of space group P2₁. Unit cell dimensions are $\text{a = 64·4}\text{A}\text{?}\text{, b = 60·6}\text{A}\text{?}\text{, c = 62·8}\text{A}\text{?}$, and β = 91·25 °. There are two molecules of molecular weight 29,000 per asymmetric unit.     

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.     

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.     

Letter: Preliminary crystallographic data for Escherichia coli beta-lactamase

The β-lactamase (penicillinase) from Escherichia coli W3310 has been crystallized from 25% saturated ammonium sulfate solution at pH 6.9. An X-ray examination of the monoclinic crystals shows the space group is C2, with unit cell dimensions $\text{a = 47.2}\text{A}\text{?}$, $\text{b = 76.9}\text{A}\text{?}$, $\text{c = 73.3}\text{A}\text{?}$ and β = 98.6°. With Z = 4 and the molecular weight = 22,000 (Melling &; Scott, 1972), the ų/dalton ratio is 2.98. The crystals are suitable for structure analysis to at least 2.4 Å resolution.     

Particle and crystal symmetry of erysimum latent virus

Erysimum latent virus, a tymovirus, contains 180 protein subunits arranged in a T = 3 icosahedral surface lattice. A cubic crystal form (with space group P2₁3 and $\text{a = 414}\text{A}\text{?}$) and a monoclinic form (space group B2, $\text{a = 442}\text{A}\text{?}\text{, b = 422}\text{A}\text{?}\text{, c = 387}\text{A}\text{?}\text{, γ = 95 °}$) have been observed. The asymmetric units of the two crystal forms contain one-third and one whole virus particle, respectively. Two possible packing arrangements of the virus particles in the monoclinic unit cell have been deduced from the low-angle diffraction patterns. X-ray diffraction data from the monoclinic crystals extend to at least 3·7 Å resolution.     

Crystallographic studies of immunoglobulins: crystallization of the Fc fragment of rabbit IgG with and without cleavage of the inter-chain disulphide bridge

The Fc fragment was prepared from rabbit immunoglobulin G by digestion with papain, both with the inter-chain disulphide bond intact, and after reduction and alkylation. These two types of Fc crystallized in different, yet related forms, each with one dimer in the asymmetric unit. The covalently linked dimer crystallized in space group $\text{P2}{}_1\text{; a = 68.85 ± 0.05}\text{A}\text{?}\text{, b = 72.50 ± 0.05}\text{A}\text{?}\text{, c = 60.40 ± 0.05}\text{A}\text{?}$ and β = 105.1 ± 0.2 °. The reduced, non-covalently linked dimer also crystallized in space group $\text{P2}{}_1\text{; a = 81.55 ± 0.05}\text{A}\text{?}\text{, b = 55.65 ± 0.05}\text{A}\text{?}\text{, c = 68.85 ± 0.05}\text{A}\text{?}$ and β = 1051 ± 0.2 °. A non-crystallographic 2-fold axis relating the two identical polypeptide chains is clearly visible in the h0l projection of the second crystal form.     

Binding of a simian virus 40 T antigen-related protein to DNA

Crystals of the periplasmic galactose-binding protein of Salmonella typhimurium have been subjected to X-ray analysis. The crystals grow as elongated rectangular prisms, with the symmetry of space group C2. Unit cell dimensions are $\text{a = 119·7}\text{A}\text{?}\text{, b = 37·2}\text{A}\text{?}\text{, c = 80·1}\text{A}\text{?}\text{, and}\text{β = 123·4}$. There is one protein molecule of molecular weight 33,000 per asymmetric unit.     

Crystallization and preliminary crystallographic data for cytochrome c551.5 (c7) from Desulfuromonas acetoxidans.

Cytochrome c₇, a low potential, three heme-containing protein (molecular weight 9800) was isolated from Desulfuromonas acetoxidans and crystallized from polyethylene glycol solutions. The crystals belong to the orthorhombic space group P2₁2₁2₁, with unit-cell dimensions $\text{a = 44·10}\text{A}\text{?}\text{, b = 37·55}\text{A}\text{?}$ and $\text{c = 45·08}\text{A}\text{?}$ and have one molecule of protein per asymmetric unit.     

Preliminary x-ray diffraction studies on the "goose-type" lysozyme from the egg-white of the black swan Cygnus atratus

The “goose-type” lysozyme isolated from the egg-white of the black swan Cygnus atratus has been crystallized. The space group is P2₁ with one molecule of protein in the asymmetric unit. The cell parameters are $\text{a = 46.2}\text{A}\text{?}\text{, b = 65.1}\text{A}\text{?}\text{, c = 38.7}\text{A}\text{?}$, β = 110 °. The crystals diffract to a resolution of 2.25 Å and a set of diffraction data for the native protein has been collected photographically.     

Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4

A tryptic core (residues 22 to 253) of the single-stranded DNA binding protein, or gene 32 protein, of bacteriophage T4 has been crystallized in four different crystal forms. One of these forms appears suitable for high-resolution X-ray crystallographic studies. It is triclinic, space group PI, with $\text{a = 67.7}\text{A}\text{?}\text{, b = 67.8}\text{A}\text{?}\text{, c = 66.0}\text{A}\text{?}\text{, α = 101.6 °, β = 107.0 °, γ = 105.2 °}$. There appear to be three protein protomers in a near-rhombohedral packing in the unit cell.     

Crystallization and preliminary X-ray diffraction studies of colicin E3 immunity protein

Immunity protein, an inhibitor of the ribonuclease activity of the protein antibiotic colicin E₃, crystallizes in the orthorhombic space group C222 with cell dimensions $\text{a = 78·7}\text{A}\text{?}\text{, b = 54·1}\text{A}\text{?}\text{, c = 36·1}\text{A}\text{?}$ and one molecule of M_r 9800 per asymmetric unit. The crystals are suitable for high resolution X-ray analysis.     

Crystallization and preliminary X-ray diffraction studies of soybean agglutinin

Soybean agglutinin crystallizes in the monoclinic space group C2 with unit cell dimensions $\text{a = 118.6}\text{A}\text{?}\text{, b = 88.9}\text{A}\text{?}\text{, c = 165.9}\text{A}\text{?}\text{, β = 103.0 °}$ and one tetramer of 120,000 M_r per asymmetric unit. The crystals are suitable for high-resolution work.     

Crystallographic study of plastocyanins

Crystals of plastocyanins from pea and corn leaves have been obtained. Both are suitable for X-ray structure analysis with a resolution up to 1.8 Å. The crystal form of plastocyanin from pea leaves belongs to the space group P2₁2₁2₁ with unit cell dimensions: $\text{a = 49.0}\text{A}\text{?}\text{, b = 53.3}\text{A}\text{?}\text{, c = 82.6}\text{A}\text{?}$. The assumed number of protein molecules per asymmetric unit of the unit cell is two. Crystals of the oxidized (Cu²⁺) and reduced (Cu⁺) forms are isomorphic. No essential differences in spot intensities for the main zone with a resolution of 3 Å were revealed. The crystal form of plastocyanin from corn leaves belongs to the space group P1 with unit cell parameters: $\text{a = 24.8}\text{A}\text{?}\text{, b = 30.0}\text{A}\text{?}\text{, c = 58.5}\text{A}\text{?}$ and α = 96° 10′, β = 87°08′, γ = 78°40′. The assumed number of protein molecules per asymmetric unit is two.     

A preliminary crystallographic investigation of rabbit muscle creatine kinase

Three crystal forms of rabbit muscle creatine kinase have been grown, one of which seems suited to a high resolution X-ray diffraction study. The first form is of monoclinic space group P2₁ with $\text{a = 54}\text{A}\text{?}\text{, b = 114}\text{A}\text{?}\text{, c = 145}\text{A}\text{?}\text{, β = 91 °}$ and has as the asymmetric unit two molecules of total molecular weight 160, 000. The second form, grown in the presence of mercurials, is of space group A2 with $\text{a = 52}\text{A}\text{?}\text{, b = 165}\text{A}\text{?}\text{, c = 237}\text{A}\text{?}\text{, β = 91 °}$ and also has two molecules in the asymmetric unit. The third crystal form, grown in the presence of a high concentration of cysteine, is of apparent space group P2₁2₁2₁, but evidence indicates that the true space group may be P2₁22₁. The dimensions of the orthorhombic unit cell are $\text{a = 47}\text{A}\text{?}\text{, b = 86}\text{A}\text{?}\text{, c = 125}\text{A}\text{?}$, and the asymmetric unit contains a single protein subunit. Assuming the latter space group, then the creatine kinase molecule possesses a twofold axis relating two identical subunits.     

Letter: Packing of microfibrils in collagen

X-ray diffraction data obtained from rat tail tendon can be indexed on a tetragonal unit cell with $\text{a = 2 × 38·47}\text{A}\text{?}$, $\text{c = 4 × 670}\text{A}\text{?}$, space group P4₁ or P4₃, in which all the intermicrofibril contacts are quasi-equivalent.     

Preliminary x-ray study of crystals of mitogenic lectin from pea seeds.

Crystals of mitogenic lectin from pea seeds (Pisum sativum) have been grown. The crystals are in space group P2₁2₁2₁ with unit cell dimensions: $\text{a = 51.0 ± 0.2}\text{A}\text{?}\text{, b = 617 ± 0.2}\text{A}\text{?}\text{, c = 137.6 ± 0.5}\text{A}\text{?}$. The asymmetric unit has one protein molecule.