Human procathepsin L has been expressed in the yeast Pichiapastoris and its inactive (Cys25Ser) and unglycosylated (ThrllOAla) mutant purified, concentrated to 4 mglml, and crystallized by vapor diffusion against solution containing 1.4 M (Na,K)PO, buffer, pH 7.8. Crystal size was increased by multi
Crystallization and preliminary X-ray diffraction studies of the human major histocompatibility antigen HLA-B27
✍ Scribed by Joan C. Gorga; Dean R. Madden; John K. Prendergast; Dr. Don C. Wiley; Jack L. Strominger
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 392 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The class I major histocompatibility (MHC) antigen HLA‐B27 was purified by immunoaffinity chromatography from the homozygous human B lymphoblastoid cell line LG‐2. Detergent‐soluble HLA‐B27 was cleaved with the protease papain to remove the hydrophobic transmembrane region and the cytoplasmic tail. Crystals of the resulting water‐soluble extracellular fragments were obtained in hanging drops by the vapor‐diffusion method. The crystals are triclinic, space group __P__1, with unit cell dimensions a = 45.9 Å, b = 71.0 Å, c = 83.7 Å, α = 79.4°, β = 88.5°, γ = 89.9°, and diffract beyond 2.5 Å resolution.
📜 SIMILAR VOLUMES
## Abstract Nonglycosylated α‐amylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2‐methyl‐2,4‐pentanediol as the precipitant in the presence of CaCl~2~ at pH 9.0. The crystals are orthorhombic, space group __P__2~1~2~1~2~1~ with unit cel
## Abstract Recombinant human adenovirus serotype 2 proteinase (both native and selenomethionine‐substituted) has been crystallized in the presence of the serotype 12, 11‐residue peptide cofactor. The crystals (space group P3~1~21 or P3~2~21, one molecule per asymmetric unit, __a = b__ = 41.3 Å, __
## Abstract Different crystal forms of the C23A mutant from the leader proteinase of foot‐and‐mouth disease virus were obtained by the hanging drop vapor diffusion technique, using MgCl~2~ and PEG 6000 as precipitants. Well‐developed crystals, with cubic morphology growing to approximately 1.0 mm^3
## Abstract A cold‐active α‐amylase was purified from culture supernatants of the antarctic psychrophile __Alteromonas haloplanctis__ A23 grown at 4 °C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold‐adapted enzyme have
Expression of the Saccharomyces cerevisiae Hsp82 chaperone in a pep4-3and hsc82-deficient strain of S. cerevisiae yielded over 25% of the total cell protein as intact Hsp82. Similarly, the amino-terminal domain (residues 1-220) of Hsp82 was expressed to 18% of the total cell protein. Crystals of the