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.     

Preliminary crystallographic data for glycolate oxidase from spinach.

Glycolate oxidase, an enzyme that plays an important role in photorespiration in plants, has been purificant from spinach and crystallized in two different crystal forms. Form A which was obtained with tertiary butanol as precipitating agent belongs to space group I 422 with unit cell dimensions a = b = 148.1 A and c = 134.9 A. This form diffracts to high resolution and will be used for further crystallographic studies. Form B is also tetragonal, space group P42212, with cell dimensions a = b = 145.4 A and c = 104.2 A. This form was obtained from ammonium sulfate precipitations. Sodium dodecyl sulfate polyacrylamide gel electrophoresis shows that the enzyme is built up from subunits of molecular weight 37,000. The asymmetric units of both crystal forms contain at least two such subunits.     

Preparation of human manganese superoxide dismutase by tri-phase partitioning and preliminary crystallographic data

Human liver manganese superoxide dismutase has been purified by a short procedure that includes a tri-phase partitioning step to provide materials that can be crystallized from ammonium sulfate. X-ray diffraction studies at 3 A resolution show that the crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with cell dimensions a = b = 81.1 A, c = 242.2 A. Manganese superoxide dismutase levels as determined by enzymatic assay as well as by enzyme-linked immunosorbent assay indicated that considerable variations occur in different livers but the total superoxide dismutase activity (Mn superoxide dismutase plus Cu,Zn superoxide dismutase) seems to be kept at constant values.     

Preliminary crystallographic data for beta-lytic protease

Beta-lytic protease from Myxobacter 495 was crystallized by dialysis with 1 m-sodium chloride and 0.1 m-sodium citrate (pH 5.95). The crystals were rhombic prisms with space group P2₁2₁2₁ and unit cell parameters a = 54.1, b = 99.6 and $\text{c = 53.9}\text{A}\text{?}$. Considerations of the cell volume and molecular weight indicate two molecules of beta-lytic protease in the asymmetric unit.     

Preliminary crystallographic data for protease omega

Protease omega from Carica papaya L. has been purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12), with a = 7.42 +/- 0.02 nm, c = 7.79 +/- 0.02 nm with one molecule in the asymmetric unit. The crystals diffract to 0.19-nm resolution using synchrotron radiation.     

Preliminary crystallographic data for transketolase from yeast

Crystals of the vitamin B1-dependent enzyme transketolase from baker's yeast have been grown from the apo- and the holoform of the enzyme, using PEG as precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell constants a = 76.3 A, b = 114.2 A, and c = 163.5 A. The crystals are stable in the x-ray beam and diffract to at least 2.2 A on a conventional x-ray source. The enzyme is a dimer of identical subunits, and a Vm value of 2.2 A/dalton indicates that the asymmetric unit contains a dimer. Rotation function calculations using native data (10-5 A) revealed a local 2-fold rotation axis with phi = 0 degree and omega = 20 degrees.     

Letter: Studies on histidinol dehydrogenase preliminary crystallographic data

Crystals of histidinol dehydrogenase (EC 1.1.1.23) from Salmonella typhimurium have been obtained in large size suitable for single crystal X-ray studies. The following crystal data were obtained on examination of a number of X-ray precession photographs; crystal system monoclinic, $\text{a = 149.6}\text{A}\text{?}$, $\text{b = 88.9}\text{A}\text{?}$, $\text{c = 105.6}\text{A}\text{?}$, β = 124.5 °, space group C2. The density of the crystal measured by flotation in bromobenzene/xylene mixture is 1.186 g/cm³. There is one dimer molecule of molecular weight 80,000 in one crystallographically asymmetric unit.     

Letter: crystallographic data fro lysoxyme from bacteriophage T4

The lysozyme of bacteriophage T4 has been crystallized in a form suitable for X-ray diffraction analysis. The space group is P3₁21 or enantiomorph, and the cell dimensions are $\text{a = b = 61.1}\text{A}\text{?}$, $\text{c = 96.3}\text{A}\text{?}$.     

Crystallization and preliminary crystallographic analysis of manganese superoxide dismutase from Bacillus halodenitrificans

Manganese superoxide dismutase (GP-MnSOD), a component of the so-called 'green protein' (green protein complex) from the facultative anaerobic halodenitrifier Bacillus halodenitrificans, has been crystallized using the hanging-drop vapor diffusion method. Crystals have unit-cell parameters a=b=93.4 A, c=65.0 A, and belong to the space group P4(3)2(1)2. Preliminary analysis indicates there is one monomer in each asymmetric unit. The structural information from this enzyme will enrich our knowledge on its high catalytic activity and its possible role in green protein complex.     

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.     

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.     

Preliminary crystallographic data for Bowman-Birk inhibitor from soybean seeds.

A well characterized soybean protease inhibitor, the Bowman-Birk inhibitor, has been crystallized at room temperature in the presence of polyethylene glycol 4000 by vapor diffusion against an ammonium sulfate solution containing 2-methyl-2,4-pentanediol. An x-ray diffraction study reveals that the inhibitor crystallizes in a hexagonal unit cell of symmetry P6122 (or P6522) and dimensions a = b = 91.36(2) A and c = 63.92(2) A. Each of the 12 asymmetric units contains 2 molecules of molecular weight 8000. The crystal, which diffracts barely to 3-A spacings, is fairly stable to x-irradiation and has a solvent content of approximately 52% by volume.     

Preliminary crystallographic data for lysozyme produced by Streptomyces erythraeus.

Crystals of lysozyme from Streptomyces erythraeus are orthorhombic, space group P2₁2₁2₁ with unit cell dimensions: $\text{a = 50.01}\text{A}\text{?}\text{, b = 61.98}\text{A}\text{?}$ and $\text{c = 67.85}\text{A}\text{?}$; and one molecule, of molecular weight about 18,500, per asymmetric unit.