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Database error: Invalid SQL: select count(id) from pwn_comment where pid='602120' and iffb='1'
MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select count(id) from pwn_comment where pid='602120' and iffb='1') called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select count(id) from {P}_comment where pid='602120' and iffb='1') called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:65] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
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Warning: mysql_query() [function.mysql-query]: Unable to save result set in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 50
Database error: Invalid SQL: select * from pwn_comment where pid='602120' and iffb='1' order by id limit 0,10
MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select * from pwn_comment where pid='602120' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select * from {P}_comment where pid='602120' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:167] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php on line 61
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发布于:2018-10-19 15:12:33  访问:63 次 回复: 篇
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Vance 900 spectrometer, working at a 900.13-MHz frequency and equipped
The amino acid substitutions were introduced, avoiding the usage of rare codons for arginine. The three synthetic genes were purchased from GeneArt (Invitrogen) to include NdeI and XhoI restriction web sites at the 5= and 3= ends, respectively. Every single gene was digested with NdeI/XhoI and cloned into the corresponding web-sites of your pET21b( ) vector (Novagen). The expression vectors have been transformed into E. coli BL21(DE3). The recombinant cells were grown at 37 to an optical density at 600 nm of 0.5, PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/22610350 at which time 1 mM isopropyl-D-thiogalactopyranoside (IPTG) was added, and also the cultures have been permitted to develop for 3 h. Cells were harvested by centrifugation at four,000 rpm for 15 min at four . Protein purification. Bacterial pellets were WZ4003 chemical information resuspended in ten ml of buffer A (50 mM NaH2PO4 [Sigma], 300 mM NaCl [Fluka], 30 mM imidazole [Merck] [pH 8.0]), sonicated, and centrifuged at 35,000 g for 30 min. The supernatant was collected and subjected to two serial purification methods XAV-939Protocol working with metal affinity chromatography (IMAC) and ionic exchange chromatography having a desalting step in among. All purification measures had been performed employing an TAxpress chromatographic method, and the OD280 was monitored. For the IMAC purification step, filtered supernatants were automatically injected into 1-ml Ni2 -HiTrap HP columns at a flow price of 1 ml/min, and the columns were washed with 20 column volumes (CV) of washing buffer (50 mM NaH2PO4 [Sigma], 300 mM NaCl [Fluka], 30 mM imidazole [Merck] [pH 8.0]). Subsequent, the His tag fusion proteins had been eluted with 5 CV of elution buffer (50 mM NaH2PO4, 300 mM NaCl, 500 mM imidazole [pH eight.0]) and automatically loaded on three 5-ml HiTrap (GE) desalting columns connected in series and eluted at a flow rate of five ml/min in 50 mM Tris-HCl (pH 8.0). For ionic exchange chromatography, the eluted proteins had been automatically loaded on 1-ml HiTrap Q HP columns at a flow price of 1 ml/min. Subsequently, the column was washed with 10 CV of 50 mM Tris-HCl (pH 8.0). The elution was setup within a linear gradient, in between 50 mM Tris-HCl (pH eight.0) and 50 mM Tris-HCl and 1.0 M NaCl (pH 8.0) buffer in 10 CV, and 1-ml fractions had been collected. Protein purity was 95 for all samples, as by determined by densitometry analyses of a SDS-PAGE 12 gel. Protein aggregation and apparent molecular weight were checked by analytical size exclusion chromatography (Waters Acquity ultraperformance liquid PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/24475050 chromatography [UPLC] system equipped having a BEH200 1.7-mm column, 4.six by 300 mm [Waters], 150 mM NaH2PO4 buffer [pH 7.0], at a flow rate of 0.4 ml/min).Vance 900 spectrometer, functioning at a 900.13-MHz frequency and equipped using a cryogenically cooled probe. Titrations were performed on 0.four mM 2H/15N-labeled fHbp 1.1 protein samples together with the unlabeled JAR5 as much as an fHbp-to-JAR5 molar ratio of 1:1.5. 1H and 15N resonance assignments for the fHbp subvariant 1.1 protein were already available (27).
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