Biological Crystallography

 

Acta Cryst. (2001). D57, 479  [ doi:10.1107/S0907444901001214 ]

To save crystallization data

B. Lorber

Synopsis: The idea of saving crystallization data of biological macromolecules in a database, as are atomic coordinates, is discussed.

Online April 2001

 

Acta Cryst. (2001). D57, 480-487  [ doi:10.1107/S0907444901000373 ]

Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution

J. W. O'Neill, D. E. Kim, D. Baker and K. Y. J. Zhang

Synopsis: Structures of a tryptophan-containing variant of the IgG-binding B1 domain of protein L have been solved in the presence and absence of zinc. The binding of zinc ions immobilized the N-terminal histidine tag and enabled the determination of the structural conformation of the histidine tag and its zinc coordination scheme. A methyl-sized cavity was found in these structures, which may explain the greater than expected destabilizing effect of several mutants.

PDB references: 1hz5 and 1hz6

Online April 2001

 

Acta Cryst. (2001). D57, 488-497  [ doi:10.1107/S0907444901000646 ]

Atomic resolution structures of trypsin provide insight into structural radiation damage

H.-K.S. Leiros, S. M. McSweeney and A. O. Smalås

Synopsis: Structural radiation damage has been examined for two high-resolution trypsin structures at 0.95 and 1.00 Å. The high intensity of ID14-EH4 at ESRF is most harmful to cryocooled protein crystals, as disulfide bonds are broken and more alternate conformations are found.

PDB references: 1hj8 and 1hj9

Online April 2001

 

Acta Cryst. (2001). D57, 498-505  [ doi:10.1107/S0907444901001147 ]

Three-dimensional structure of human RNase 1N7 at 1.9 Å resolution

J. Pous, G. Mallorquí-Fernández, R. Peracaula, S. S. Terzyan, J. Futami, H. Tada, H. Yamada, M. Seno, R. de Llorens, F. X. Gomis-Rüth and M. Coll

Synopsis: The structure of human pancreatic RNase contributes to the development of new applications in cancer diagnostics.

PDB reference: 1e21

Online April 2001

 

Acta Cryst. (2001). D57, 506-515  [ doi:10.1107/S0907444901001925 ]

The structure of human mitochondrial branched-chain aminotransferase

N. Yennawar, J. Dunbar, M. Conway, S. Hutson and G. Farber

Synopsis: X-ray crystal structures of three forms of human mitochondrial branched-chain aminotransferase were solved by molecular-replacement methods. In two of the forms the enzyme is in its active form, with the pyridoxal 5'-phosphate (PLP) cofactor covalently linked to the -amino group of the active-site lysine. In the third form, a molecule of the Tris buffer is covalently bound to the PLP on one end and the active-site lysine on the other, inhibiting the enzyme irreversibly.

PDB references: 1ekf, 1ekv and 1ekp

Online April 2001

 

Acta Cryst. (2001). D57, 516-526  [ doi:10.1107/S0907444901002530 ]

X-ray structure of bovine pancreatic phospholipase A₂ at atomic resolution

R. A. Steiner, H. J. Rozeboom, A. de Vries, K. H. Kalk, G. N. Murshudov, K. S. Wilson and B. W. Dijkstra

Synopsis: The crystal structure of bovine pancreatic phospholipase A₂ has been refined to 0.97 Å resolution. The structure presents flexibility at the surface where the key interfacial recognition site is located; a cluster of MPD molecules near the active site was visualized and the modelled solvent region was expanded.

PDB reference: 1g4i

Online April 2001

 

Acta Cryst. (2001). D57, 527-535  [ doi:10.1107/S0907444901002554 ]

Structures and comparison of the Y98H (2.0 Å) and Y98W (1.5 Å) mutants of flavodoxin (Desulfovibrio vulgaris)

R. A. Reynolds, W. Watt and K. D. Watenpaugh

Synopsis: Two mutants of D. vulgaris flavodoxin, Y98H and Y98W, have been solved to 2.0 and 1.5 Å, respectively. A comparison is made between the two mutants and the different oxidation states of the native flavodoxin.

PDB references: 1i1o and 1f4p

Online April 2001

 

Acta Cryst. (2001). D57, 536-544  [ doi:10.1107/S0907444901001652 ]

Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain

V. Molteni, J. Greenwald, D. Rhodes, Y. Hwang, W. Kwiatkowski, F. D. Bushman, J. S. Siegel and S. Choe

Synopsis: Here, the identification by X-ray crystallography of a small-molecule binding site on the integrase catalytic domain is reported. The small-molecule family studied consists of a core of arsenic or phosphorus surrounded by four aromatic groups.

PDB references: 1hyv and 1hyz

Online April 2001

 

Acta Cryst. (2001). D57, 545-551  [ doi:10.1107/S0907444901002529 ]

Structure of the C-terminal sterile -motif (SAM) domain of human p73

W. K. Wang, M. Bycroft, N. W. Foster, A. M. Buckle, A. R. Fersht and Y. W. Chen

Synopsis: The structure of human p73 SAM domain has the five-helix bundle fold that is characteristic of all SAM-domain structures, with an overall r.m.s.d. of 1.5 Å for main-chain atoms compared with the solution structure. Several unusual structural features that might have functional implications are described.

PDB reference: 1dxs

Online April 2001

 

Acta Cryst. (2001). D57, 552-558  [ doi:10.1107/S0907444901001743 ]

Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermus thermophilus aspartyl-tRNA synthetase-1

D.-W. Zhu, B. Lorber, C. Sauter, J. D. Ng, P. Bénas, C. Le Grimellec and R. Giegé

Synopsis: A novel crystal form of T. thermophilus aspartyl-tRNA synthetase (AspRS-1) prepared in the presence of polyethylene glycol and agarose is suitable for structure determination at high resolution.

Online April 2001

 

Acta Cryst. (2001). D57, 559-565  [ doi:10.1107/S0907444901001202 ]

Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

S. Weinkauf, J. F. Hunt, J. Scheuring, L. Henry, J. Fak, D. B. Oliver and J. Deisenhofer

Synopsis: The SecA translocation ATPase acts as a molecular motor which drives the translocation of proteins through bacterial membranes. In doing so it undergoes large conformational changes and this flexibility may hinder crystallization of the protein. Stabilization of this protein's conformation and its crystallization have been achieved using high glycerol concentrations.

Online April 2001

 

Acta Cryst. (2001). D57, 566-573  [ doi:10.1107/S0907444901001196 ]

Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures

M. Weik, G. Kryger, A. M. M. Schreurs, B. Bouma, I. Silman, J. L. Sussman, P. Gros and J. Kroon

Synopsis: Solvent behaviour in flash-cooled protein crystals was assessed by monitoring the expansion of unit-cell parameters as a function of temperature. Solvent in large channels undergoes a glass transition and crystallizes at 155 K.

Online April 2001

 

Acta Cryst. (2001). D57, 574-578  [ doi:10.1107/S0907444901001123 ]

Map self-validation: a useful discriminator of phase correctness at low resolution

D. A. Langs, R. H. Blessing and D. Guo

Synopsis: A new map-validation procedure based on the correlation-coefficient agreement between the observed structure-factor magnitudes and their extrapolated values from suitably modified electron-density maps from which they have been each in turn systematically excluded is presented.

Online April 2001

 

Acta Cryst. (2001). D57, 579-581  [ doi:10.1107/S0907444900019314 ]

Crystallization of Clonorchis sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengths

Y.-H. Han, Y.-H. Chung, T.-Y. Kim, S.-J. Hong, J.-D. Choi and Y. J. Chung

Synopsis: Single crystals of C. sinensis 26 kDa glutathione S-transferase and its fusion proteins with peptides of different lengths have been grown in the same crystal form under similar crystallization conditions.

Online April 2001

 

Acta Cryst. (2001). D57, 582-585  [ doi:10.1107/S0907444901000439 ]

Crystallization and preliminary X-ray analysis of dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600

B. A. Manjasetty, N. Croteau, J. Powlowski and A. Vrielink

Synopsis: DmpFG-encoded 4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylating) from Pseudomaonas sp. strain CF600 has been crystallized and data collected to 2.1 Å resolution. Three isomorphous heavy-atom derivatives have been identified.

Online April 2001

 

Acta Cryst. (2001). D57, 586-588  [ doi:10.1107/S0907444901001007 ]

Expression, purification and preliminary crystallographic studies of human ketohexokinase

M. Kozak, B. Hayward, D. Borek, D. T. Bonthron and M. Jaskólski

Synopsis: Human ketohexokinase has been produced in E. coli, purified and crystallized in an orthorhombic form (space group P2₁2₁2 or P2₁2₁2₁) with four protein molecules in the asymmetric unit.

Online April 2001

 

Acta Cryst. (2001). D57, 589-591  [ doi:10.1107/S0907444901001160 ]

Crystallization and preliminary X-ray crystallographic analysis of the human type 3 3-hydroxysteroid dehydrogenase at 1.8 Å resolution

D.-W. Zhu, L. Cantin, V. Nahoum, P. Rehse, V. Luu-The, F. Labrie, R. Breton and S.-X. Lin

Synopsis: Human type 3 3-hydroxysteroid dehydrogenase has been crystallized in ternary complex with testosterone and NADP⁺ and diffracts to 1.6 Å.

Online April 2001

 

Acta Cryst. (2001). D57, 592-595  [ doi:10.1107/S0907444901001238 ]

Human phosphoglucose isomerase: expression, purification, crystallization and preliminary crystallographic analysis

A. T. Cordeiro, P. H. C. Godoi, L. F. Delboni, G. Oliva and O. H. Thiemann

Synopsis: The human phosphoglucose isomerase (PGI) enzyme has been overproduced in the heterologous E. coli expression system and crystallized, allowing its X-ray structure determination.

Online April 2001

 

Acta Cryst. (2001). D57, 596-598  [ doi:10.1107/S0907444901001342 ]

Structural studies on the cobra venom factor: isolation, purification, crystallization and preliminary crystallographic analysis

S. Sharma, T. Jabeen, R. K. Singh, R. Bredhorst, C.-W. Vogel, Ch. Betzel and T. P. Singh

Synopsis: Cobra venom factor, a three-chain complement-activating glycoprotein, has been crystallized for the first time. The crystals belong to space group P4₁ with unit-cell dimensions a = b = 62.7, c = 368.1 Å and diffract to at least 2.7 Å resolution.

Online April 2001

 

Acta Cryst. (2001). D57, 599-601  [ doi:10.1107/S0907444901001639 ]

Crystallization and preliminary crystallographic studies of a phospholipase A₂ from the venom of the Brazilian snake Bothrops moojeni

M. C. Nonato, R. C. Garratt, Y. P. Mascarenhas, W. D. P. Jesus, M. T. Assakura, S. M. T. Serrano and G. Oliva

Synopsis: A phospholipase A₂ from the venom of B. moojeni has been crystallized and data have been collected to 2.35 Å. The structure was solved by molecular-replacement techniques.

Online April 2001

 

Acta Cryst. (2001). D57, 602-604  [ doi:10.1107/S0907444901001810 ]

Preliminary crystallographic studies of EcTI, a serine proteinase inhibitor from Enterolobium contortisiliquum seeds

I. F. C. Batista, M. C. Nonato, M. R. Bonfadini, L. M. Beltramini, M. L. V. Oliva, M. U. Sampaio, C. A. M. Sampaio and R. C. Garratt

Synopsis: This report describes for the first time the preliminary crystallographic and structural studies of EcTI (E. contortisiliquum trypsin inhibitor), a plant Kunitz trypsin inhibitor composed of two polypeptide chains. EcTI has properties such as inhibition of blood clotting and fibrinolytic enzymes (factor XIIa and plasmin) which are not shared by other members of the same family of known structure.

Online April 2001

 

Acta Cryst. (2001). D57, 605-608  [ doi:10.1107/S0907444901001895 ]

Crystallization and functional analysis of a soluble deglycosylated form of the human costimulatory molecule B7-1

S. J. Davis, S. Ikemizu, A. V. Collins, J. A. Fennelly, K. Harlos, E. Y. Jones and D. I. Stuart

Synopsis: B7-1 is a heavily glycosylated cell-surface molecule and a key target for human immunotherapy. Detailed methods for crystallizing this important but difficult protein are presented.

Online April 2001

 

Acta Cryst. (2001). D57, 609-611  [ doi:10.1107/S0907444901002104 ]

The crystals of a mannose-specific jacalin-related lectin from Morus nigra are merohedrally twinned

A. Rabijns, C. Verboven, H. Novoa de Armas, E. J. M. Van Damme, W. J. Peumans and C. J. De Ranter

Synopsis: Preliminary X-ray data of the unbound and mannose-bound forms of MornigaM, a mannose-specific jacalin-related lectin from M. nigra, show the tetrameric assembly of this protein.

Online April 2001

 

Acta Cryst. (2001). D57, 612-613  [ doi:10.1107/S0907444901002141 ]

Crystallization and preliminary X-ray crystallographic analysis of the surE protein from Thermotoga maritima

J. E. Kwak, K. S. Ha, J. Y. Lee, Y. J. Im, S. H. Park, S. H. Eom and S. W. Suh

Synopsis: Homologues of the E. coli surE protein are well conserved among both the eubacteria and the archaea. The surE protein from T. maritima has been crystallized and diffraction data have been collected to 1.9 Å resolution.

Online April 2001

 

Acta Cryst. (2001). D57, 614-615  [ doi:10.1107/S0907444901001226 ]

Purification, crystallization and preliminary X-ray studies of thermostable alkaline phosphatase from Thermus sp. 3041

C.-N. Ji, T. Jiang, M.-Q. Chen, X.-Y. Sheng and Y.-M. Mao

Synopsis: Thermostable alkaline phosphatase from Thermus sp. 3041 has been expressed in E. coli, purified and crystallized. The crystals belong to space group P2₁22₁, with unit-cell parameters a = 57.7, b = 69.9, c = 111.5 Å.

Online April 2001

 

Acta Cryst. (2001). D57, 616-617  [ doi:10.1107/S0907444901001937 ]

Crystallization and preliminary X-ray diffraction studies of the guanylate kinase-like domain of PSD-95 protein from rat

J. J. Kim, S.-H. Rho, Y. J. Im, E. J. Kim and S. H. Eom

Synopsis: The guanylate kinase-like domain of PSD-95 from R. norvegicus has been crystallized in a form suitable for X-ray diffraction studies. The crystals belong to space group P4₃ (or P4₁) and diffract to 2.35 Å.

Online April 2001