Crystallization of ribonuclease St

The crystals of ribonuclease St, the extracellular ribonuclease from Streptomyces erythreus, have been obtained from (NH₄)₂SO₄ solution with acetate buffer (pH 4.1). The crystals belong to a monoclinic space group C2 with dimensions $\text{a = 88.4}\text{A}\text{?}\text{, b = 33.0}\text{A}\text{?}\text{, c = 69.0}\text{A}\text{?}\text{, β = 98.4 °}$. There are two protein molecules per asymmetric unit. The crystals diffract beyond 2.0 Å resolution.     

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.     

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.     

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.     

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.     

Preliminary crystallographic study of omega-amino acid: pyruvate aminotransferase from Pseudomonas sp. F-126.

Large single crystals of ω-amino acid: pyruvate aminotransferase, were prepared by dialysis of the enzyme solution against 2.2 m-ammonium sulphate solution at pH 7.8. X-ray diffraction patterns show that the crystals belong to the orthorhombic space group I222 or I2₁2₁2₁ with unit cell dimensions $\text{a = 124.1}\text{A}\text{?}\text{, b = 137.9}\text{A}\text{?}\text{, and}\text{c = 61.2}\text{A}\text{?}$. The asymmetric unit consists of one monomer of molecular weight 43,000.     

Preliminary X-ray study of crystals of human transferrin

Large crystals of human transferrin have been grown from polyethylene glycol solutions. The crystals are orthorhombic, space group P2₁2₁2₁, with $\text{a = 78}\text{A}\text{?}\text{, b = 94}\text{A}\text{?}\text{and}\text{c = 112}\text{A}\text{?}$. Density measurements indicate that there are four transferrin molecules in the unit cell.     

Characterization and preliminary crystallographic data on the VL-related fragment of the human kI Bence Jones protein Wat

A “naturally occurring” human κI V_L dimer, designated Wat, has been isolated and crystallized. Protein Wat consists of two non-covalently bound monomers, each having a molecular weight of ~ 11,500. The monomer subunit is composed of an entire variable region light chain (V_L) domain closely homologous to that of the κI Bence Jones protein Roy (Hilschmann &; Craig, 1965) as evidenced from amino acid composition, tryptic peptide map, and sequence analysis. Immunochemical studies substantiated that protein Wat is of the κ chain subgroup κI and lacks the isotypic and allotypic antigenic determinants associated with the κ constant region light chain domain. Two types of crystals of V_L dimer Wat were obtained from ammonium sulfate or polyethylene glycol solutions. The type I crystals have unit cell dimensions of $\text{a = b = 82.6}\text{A}\text{?}\text{, c = 60.3}\text{A}\text{?}$, and the space group is hexagonal P6₂ or P6₄. The asymmetric unit consists of one V_L dimer; the fractional volume of unit cell occupied by solvent is 0.51. The unit cell dimensions of the type II crystals are $\text{a = b = 1,08.3}\text{A}\text{?}\text{, c = 108.8}\text{A}\text{?}$; the space group is hexagonal P6₁22 or P6₅22. Three variable domains constitute the asymmetric unit of the type II crystals; the fractional value of the solvent (0.52) is compatible with the value obtained for the type I crystals.     

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.     

Crystals of myohemerythrin

Crystals have been grown of metazide myohemerythrin from the sipunculid Dendrostomum pyroides. The crystals are in space group P2₁2₁2₁ and have unit cell dimensions of $\text{a = 41.6}\text{A}\text{?}\text{, b = 80.0}\text{A}\text{?}\text{and}\text{c = 37.8}\text{A}\text{?}$. An asymmetric unit contains a single myohemerythrin molecule.     

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.     

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.     

Manganese superoxide dismutases from Escherichia coli and from yeast mitochondria: Preliminary X-ray crystallographic studies

The Mn superoxide dismutase from Escherichia coli has been obtained in three crystal forms: (I) from 68% saturated (NH₄)₂SO₄, space group P222 or P222₁, $\text{a = 47}\text{A}\text{?}\text{, b = 103}\text{A}\text{?}\text{, c = 47.5}\text{A}\text{?}$, with one subunit per asymmetric unit; (II) from 50% polyethylene glycol 6000, space group C222₁ (with approx. P4₁2₁2 symmetry), $\text{a = 101}\text{A}\text{?}\text{, b = 108}\text{A}\text{?}\text{, c = 180}\text{A}\text{?}$, with four subunits (2 molecules) per asymmetric unit; (III) from 52% polyethylene glycol with a different method of preparing the enzyme solution, space group P2₁2₁2, $\text{a = 47}\text{A}\text{?}\text{, b = 51}\text{A}\text{?}\text{, c = 188}\text{A}\text{?}$, with two subunits per asymmetric unit.The yeast mitochondrial Mn superoxide dismutase has yielded the same crystal form both from 30% 2-methyl-2,4-pentane diol and from 23% polyethylene glycol 6000: space group P2₁2₁2₁, $\text{a = 63}\text{A}\text{?}\text{, b = 115}\text{A}\text{?}\text{, c = 125}\text{A}\text{?}$, with four subunits (one molecule) per asymmetric unit.A full X-ray crystallographic study of at least one of these enzymes is planned.     

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.     

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.     

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 crystallographic data for the structure of the complex between Kazal trypsin inhibitor and trypsinogen

Crystals of the complex between porcine pancreatic secretory trypsin inhibitor (Kazal PSTI) and trypsinogen have been grown from magnesium sulphate solution at pH 6.7. The crystals belong to space group P2₁2₁2₁, with unit cell edges $\text{a = 67.1}\text{A}\text{?}\text{, b = 75.5}\text{A}\text{?}\text{, c = 66.9}\text{A}\text{?}$, and the asymmetric unit contains one complex moiety. This crystalline modification is suitable for a high-resolution crystallographic investigation.     

Preliminary X-ray investigation of fragment 1 of bovine prothrombin

Crystals of fragment 1 of bovine prothrombin grown from phosphate at pH 7.5 are tetragonal, space group P4₁2₂2 or P4₃2₁2 with $\text{a = b = 79.5}\text{A}\text{?}\text{, c = 84.9}\text{A}\text{?}$, with probably one molecule of 22,000 molecular weight in the asymmetric unit. The presence of 17.5% carbohydrate in the fragment may account for the high liquid content (60%) of the crystals.     

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.     

Preliminary crystallographic data for adenylosuccinate synthetase from rabbit skeletal muscle

Single crystals of adenylosuccinate synthetase, an essential component of purine biosynthesis, extracted from rabbit skeletal muscle were prepared as suitable specimens for X-ray structure analysis. The crystal belongs to the space group P4₃2₁2 or P4₁2₁2 with unit cell dimensions $\text{a = b = 71.2}\text{A}\text{?}\text{, c = 194.8}\text{A}\text{?}$. The asymmetric unit contains one protein molecule of 54,000 molecular weight.