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.     

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.     

Crystallographic data for a penicillin receptor : exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61.

A pencillin-sensitive enzyme, the exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61, has been crystallized from polyethylene glycol (M_r = 6000 to 7500) solution at pH 7·6. X-ray examination of the orthorhombic crystals shows the space group is P2₁2₁2₁, with unit cell dimensions $\text{a = 51·1}\text{A}\text{?}\text{, b = 67·4}\text{A}\text{?}\text{,}\text{and}\text{c = 102·9}\text{A}\text{?}$. With four molecules of molecular weight 38,000, the $\text{A}\text{?}{}^3\text{/}\text{dalton}$ ratio for the cell is 2·33. The crystals are stable to irradiation for 75 hours and are suitable for structure analysis to at least 2·4 Å resolution. The radius of gyration of the molecule in solution at pH 6.8 is 20.8 Å.     

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.     

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.     

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.     

Preliminary crystallographic data for Azotobacter cytochrome c5.

Two closely related crystal forms of dimeric cytochrome c₅ from Azotobacter rinelandii have been grown. The crystals belong to space groups (C2 with $\text{a = 45·0, b = 38·4, c = 41·3}\text{A}\text{?}\text{and}\text{β = 101 ° 0′}$; and C1 (a centered triclinic cell) with $\text{a = 46·0, b = 37·6, c = 49·4}\text{A}\text{?}$, α = 87 ° 20′, β = 96 ° 40′ and γ = 90 ° 0′. In C2 the 24,000 molecular weight dimer lies on a Crystallographic 2-fold axis; in C1 the entire dimer occupies the asymmetric unit.     

Crystallization of hen eggwhite riboflavin-binding protein

Crystals of hen eggwhite riboflavin-binding protein have been grown by equilibrium dialysis in solutions buffered with 0.05 m-Tris · HCl (pH 8.5) using ammonium sulphate as the precipitant. The crystals belong to the space group P3₁21 (or enantiomorph) with $\text{a = b = 112.5}\text{A}\text{?}\text{and}\text{c = 72.0}\text{A}\text{?}\text{,}$ and diffract to a resolution of 2.8 Å.     

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 investigation of ubiquitin, a non-histone chromosomal protein.

Large crystals of bovine thymus ubiquitin, a non-histone chromosomal protein, were grown from polyethylene glycol solutions. The crystals are orthorhombic, space group P2₁2₁2₁, with $\text{a = 50·9}\text{a}\text{?}\text{, b = 42·9}\text{A}\text{?}\text{and}\text{c = 29·0}\text{A}\text{?}$. The asymmetric unit contains one ubiquitin molecule.     

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.     

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.     

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.     

Crystallizations and preliminary X-ray studies of calotropins DI and DII

Crystals of calotropin DI (M_r 23,400), have been prepared by microdialysis against 5% (w/v) polyethylene glycol 20,000 in water, pH 7.0. They have orthorhombic space group P2₁2₁2₁ with cell parameters $\text{a = 57.5}\text{A}\text{?}\text{, b = 86.2}\text{A}\text{?}\text{, c = 40.3}\text{A}\text{?}$. Crystals of calotropin DII (M_r 24,000), prepared by the same technique against 5% (w/v) polyethylene glycol 20,000 in phosphate buffer of low ionic strength, pH 7.0, display monoclinic space group C2 with cell parameters $\text{a = 135.8}\text{A}\text{?}\text{, b = 32.0}\text{A}\text{?}\text{, c = 47.7}\text{A}\text{?}\text{, β = 103.80 °}$. In both cases, there is only one molecule in the asymmetric unit.     

Crystals of a bovine neurophysin II-dipeptide amide complex.

Bovine neurophysin II, a hormone carrier protein, has been crystallized as a binary complex with l-phenylalanyl-l-tyrosine amide, a peptide known to bind neurophysin at its hormone binding site. The crystals belong to space group P2₁2₁2₁ with cell constants of $\text{a = 121.6(10)}\text{A}\text{?}\text{, b = 67·9(6)}\text{A}\text{?}\text{and}\text{c = 62·1(6)}\text{A}\text{?}$. The density of the crystal is 1.156 g/cm³. There is a tetramer or two dimers in an asymmetric unit.     

Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g.

The dd-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (M_r 6000 to 7500) solution at pH 8.0. X-ray examination of the prismatic crystals shows that the space group is P2₁ with unit cell dimensions $\text{a = 51.1}\text{A}\text{?}\text{, b = 49.7}\text{A}\text{?}\text{, c = 38.7}\text{A}\text{?}\text{, β = 100.6 °}$ and one molecule in the asymmetric unit. A crystal suspension made in 50 mm-Tris · HCl buffer (pH 8.0) supplemented with 5 mm-MgCl₂ and 16% ($\text{w}\text{v}$) polyethylene glycol exhibits enzyme activity on the substrate Ac₂-l-Lys-d-Ala-d-Ala.     

Preliminary X-ray crystallographic study of the turkey lens protein, δ-crystallin

The structural protein, δ-crystallin, has been purified and crystallized from adult turkey lens. The crystals are orthorhombic and normally belong to space group P2₁2₁2 with unit cell dimensions $\text{a = 99.9(2)}\text{A}\text{?}\text{, b = 133.4(3)}\text{A}\text{?}\text{and}\text{c = 69.1(2)}\text{A}\text{?}$. This corresponds to two molecules of molecular weight approximately 200,000 per unit cell. A second crystal form has also been found in which b and c increase to 135.4(3) Å and 140.0(3) Å. respectively, indicating four molecules per unit cell.     

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 °.     

Highly ordered crystals of the plant seed protein crambin.

Crystals of crambin, a plant seed protein of molecular weight 5000, diffract X-rays strongly to the interplanar spacing limit of 0.88 Å. These diffraction data should allow a definition of atomic structure that is on a par with that typically obtained from crystals of small organic molecules. The crystals are in space group P2₁ and have unit cell dimensions $\text{a = 41.1}\text{A}\text{?}\text{, b = 18.7}\text{A}\text{?}\text{, c = 22·7}\text{A}\text{?}\text{,}\text{and}\text{β = 90.6 °}$. The asymmetric unit contains one protein molecule.