Match!
Alexander McPherson
University of California, Irvine
Protein crystallizationChemistryCrystallizationCrystalCrystallography
285Publications
51H-index
10.7kCitations
What is this?
Publications 282
Newest
#1Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
#2Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
Last. Andrew Kalasky (UCI: University of California, Irvine)
view all 3 authors...
Source
Abstract A sample of Apolipoprotein E3 used in the original structure determination by X-ray crystallography (PDB code 1NFN) was crystallized under different conditions and its structure determined by molecular replacement at 298° K. The original model (1NFN) began at amino acid 23 and ended at amino acid 164, but the amino acid segment 81 through 91 (a loop between helices) was not visible in the electron density and presumed disordered. The model reported here is essentially identical to 1NFN,...
Source
Abstract X-ray intensities extending to 1.4 A resolution were collected on the P63 hexagonal crystal form of canavalin, and extended to 1.9 A for the orthorhombic C2221 crystals. Structure determination of a new crystal form of canavalin having space group P212121 is reported as well. Both the N and C terminal cupin domains contained identifiable ligands. For hexagonal crystals, in the cavity of the C terminal cupin, a molecule of benzoic acid was found, bound through carboxyl oxygens to Histidi...
Source
#1Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
#2Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
Abstract The β subunit of bovine luteinizing hormone (LH) was crystallized and its structure solved to 3.15 ​A resolution by molecular replacement using human chorionic gonadotropin (hCG) β subunit as search model. The asymmetric unit contains two copies of the β subunit that are related by a non-crystallographic symmetry (NCS) two-fold axis, both copies of which contain proteolytic cleavages after amino acid 100. It is noteworthy that the oligosaccharide moieties covalently attached at asparagi...
Source
#1Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
view all 2 authors...
Abstract The β subunit of bovine luteinizing hormone (LH) was crystallized and its structure solved to 3.15 ​A resolution by molecular replacement using human chorionic gonadotropin (hCG) β subunit as search model. The asymmetric unit contains two copies of the β subunit that are related by a non-crystallographic symmetry (NCS) two-fold axis, both copies of which contain proteolytic cleavages after amino acid 100. It is noteworthy that the oligosaccharide moieties covalently attached at asparagi...
Source
#1Todd O. Yeates (UCLA: University of California, Los Angeles)H-Index: 62
#2Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
Bovine β-lactoglobulin was crystallized from 3 M NaCl buffered at pH 3.8 with sodium citrate as thick hexagonal prisms of greater than 1 mm in edge length. Analyses of the X-ray diffraction intensities using three different current algorithms were unanimous in specifying the space group to be P6322, with unit-cell dimensions a = b = 75.47, c = 140.79 A. No progress could be made, however, towards an acceptable solution by molecular replacement using this symmetry. In the end, it was found that t...
1 CitationsSource
#1Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
#2John Day (UCI: University of California, Irvine)H-Index: 11
Last. Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
view all 3 authors...
In the course of an earlier investigation into the crystallization of proteins based on the addition of intermolecular ligands, the Kunitz type trypsin inhibitor from soybean (SBTI) was crystallized as a complex with 1,5-disulfonylnaphthalene (ligand library 21D). The two molecules within the asymmetric unit of the monoclinic crystals are related by a near-exact NCS 2-fold axis and have essentially the same conformation as was found for them in previous analyses. The protein dimer is maintained ...
1 CitationsSource
#1Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
#2Jesse A. Jones (UTHSC: University of Tennessee Health Science Center)H-Index: 2
Last. Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
view all 3 authors...
An iron-containing alcohol dehydrogenase (FeADH) from the hyperthermophilic archaeon Thermococcus thioreducens was crystallized in unit cells belonging to space groups P21, P212121 and P43212, and the crystal structures were solved at 2.4, 2.1 and 1.9 A resolution, respectively, by molecular replacement using the FeADH from Thermotoga maritima (Schwarzenbacher et al., 2004) as a model. In the monoclinic and orthorhombic crystals the dehydrogenase (molecular mass 41.5 kDa) existed as a dimer cont...
Source
: Experiments were carried out on 15 different protein crystals with the objective of estimating the rates of penetration of dye molecules into the crystals. The dyes were in the molecular-weight range 250-1000 Da and the protein crystals were of dimensions of 0.7 mm or greater. Experiments were also conducted on protein crystals grown between glass cover slips (separation 200 µm) that restricted the direction of diffusion. The rate of penetration of dyes into protein crystals depends very much ...
2 CitationsSource
#1Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
#2Steven B. Larson (UCI: University of California, Irvine)H-Index: 16
Human endothelin is a 21-amino-acid polypeptide, constrained by two intra-chain disulfide bridges, that is made by endothelial cells. It is the most potent vasoconstrictor in the body and is crucially important in the regulation of blood pressure. It plays a major role in a host of medical conditions, including hypertension, diabetes, stroke and cancer. Endothelin was crystallized 28 years ago in the putative space group P6122, but the structure was never successfully solved by X-ray diffraction...
2 CitationsSource
12345678910