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1.
The N-terminal half molecule of ovotransferrin has been crystallized from a polyethylene glycol 6000 solution by means of the vapor diffusion method. The crystals belong to the orthorhombic system, space group P2(1)2(1)2(1), with cell dimension of a = 47.0, b = 90.2, and c = 76.2 A. The crystals diffract X-rays to a resolution limit of at least 2.0 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.  相似文献   

2.
Pectate lyase is a saccharide-binding enzyme that lyitically depolymerizes polypectate in higher plant cell walls, thus causing soft-rot diseases in food crops. A pectate lyase from Erwinia chrysanthemi, EC16 (PLe), crystallizes in the orthorhombic space group P2(1)2(1)2(1) with unit cell dimension of a = 39.0 A, b = 91.0 A and c = 103.4 A. The asymmetric unit consists of one molecule with a molecular mass of 38,118 daltons and the X-ray diffraction extends to a resolution of 1.8 A. The crystals reproducibly grow to large dimensions and are suitable for a high-resolution X-ray diffraction analysis.  相似文献   

3.
Haloalkane dehalogenases are enzymes that release chloride or bromide from n-halogenated alkanes. X-ray quality crystals of haloalkane dehalogenase from the 1,2-dichloroethane-degrading bacterium Xanthobacter autotrophicus GJ10 have been grown at room temperature from 64% saturated ammonium sulfate solutions (pH 6.2 to 6.4). The crystals diffract in the X-ray beam to at least 2.4 A resolution (1 A = 0.1 nm). Their space group is P2(1)2(1)2, with cell dimensions a = 94.1 A, b = 72.8 A, c = 41.4 A and alpha = beta = gamma = 90 degrees. There is one monomer (molecular weight 36,000) per asymmetric unit.  相似文献   

4.
Crystals of an ATPase fragment of bovine clathrin uncoating ATPase   总被引:1,自引:0,他引:1  
A 44,000 Mr amino-terminal, clathrin-independent ATPase fragment of the bovine clathrin uncoating ATPase has been crystallized in a form suitable for X-ray diffraction studies. The crystals are orthorhombic, space group P2(1)2(1)2(1), a = 145.3 A, b = 65.0 A, c = 46.9 A, with one protein molecule per asymmetric unit (1 A = 0.1 nm).  相似文献   

5.
Uridine diphosphogalactose-4-epimerase from E. coli has been crystallized in a form suitable for a high-resolution X-ray crystallographic structural analysis. The enzyme complexed with a substrate analogue, uridine diphosphobenzene (UDP-benzene), crystallizes readily using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 76.3 A, b = 83.1 A, and c = 132.1 A. Based on still setting photographs, the crystals diffract to a nominal resolution of 2.3 A and are stable in the X-ray beam. The enzyme used in these experiments was produced by a new expression system and a modified purification scheme.  相似文献   

6.
alpha-Amylase from Bacillus licheniformis has been crystallized by the hanging-drop vapor diffusion method in the presence of calcium ions using ammonium sulfate as precipitant. The crystals are tetragonal, belonging to the space group P4(1)2(1)2 (or P4(3)2(1)2), with unit cell dimensions of a = 119.9 and c = 85.4 A. The asymmetric unit contains one molecule of alpha-amylase, with a crystal volume per protein mass (VM) of 2.78 A3/Da. The crystals diffract to better than 2.0 A Bragg spacing when exposed to synchrotron X-rays and they are reasonably stable in the X-ray beam. Thus the crystals are suitable for structure determination at high resolution by X-ray methods.  相似文献   

7.
Human apo-lactoferrin in both native and deglycosylated forms has been purified, and crystals obtained by dialysis against low ionic strength buffer solutions. The crystals of native apo-lactoferrin are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 222.0 A, b = 115.6 A, c = 77.8 A and have two protein molecules per asymmetric unit. Two crystal forms of deglycosylated apo-lactoferrin have been obtained. One is orthorhombic, space group P2(1)2(1)2(1), with cell dimensions a = 152.1 A, b = 94.6 A, c = 55.8 A. The second is tetragonal, space group I4, with cell dimensions a = b = 189.4 A, c = 55.1 A. Both of the latter have only one molecule per asymmetric unit, and are suitable for high-resolution X-ray structure analysis.  相似文献   

8.
Crystals suitable for X-ray diffraction analysis of both glycosylated and non-glycosylated forms of a barley peroxidase have been grown. The crystals of the glycosylated peroxidase have been grown by the hanging drop vapour diffusion method using polyethylene glycol 4000 as the precipitant in the presence of n-propanol and potassium iodide at pH 8.5. The crystals are needles belonging to the orthorhombic spacegroup P2(1)2(1)2(1) with unit cell dimensions a = 62.95 A, b = 66.24 A and c = 70.78 A. There is one barley peroxidase molecule in the asymmetric unit. The crystals contain approximately 38% solvent and appear to be stable to lengthy X-ray exposure. They diffract to beyond 1.9 A.  相似文献   

9.
Crystals of D-glucose-6-phosphate: NADP+ oxidoreductase were obtained with the hanging drop, vapor diffusion and batch methods from ammonium sulfate-containing solutions. X-ray diffraction photographs indicate that the crystals belong to the orthorhombic space groups I222 or I2(1)2(1)2(1) with unit cell dimensions of a = 66.0 A, b = 140.8 A and c = 177.8 A. These data, together with results from sodium dodecyl sulfate/polyacrylamide gel electrophoresis and crystal density experiments, indicate that there is one 116,000 Mr dimer per asymmetric unit. The crystals diffract to at least 2.2 A and are suitable for X-ray crystallographic structure determination.  相似文献   

10.
The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P2(1)2(1)2(1) with one dimer in the asymmetric unit. The cell dimensions are: a = 64.2, b = 83.8, c = 193 A. X-ray reflections extend to at least 2.2 A resolution.  相似文献   

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